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        <title>International Journal of Biological Macromolecules via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'International Journal of Biological Macromolecules' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=International+Journal+of+Biological+Macromolecules&t=International+Journal+of+Biological+Macromolecules&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 13:38:35 +0100</lastBuildDate>
        <item>
            <title>Immobilization of thermoalkalophilic recombinant esterase enzyme by entrapment in silicate coated Ca-alginate beads and its hydrolytic properties.</title>
            <link>http://www.medworm.com/index.php?rid=5672241&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22309712%26dopt%3DAbstract</link>
            <description>Authors: Gülay S, Sanlı-Mohamed G
    Abstract
    Thermoalkalophilic esterase enzyme from Balçova (Agamemnon) geothermal site were aimed to be immobilized effectively via a simple and cost-effective protocol in silicate coated Calcium alginate (Ca-alginate) beads by entrapment. The optimal immobilization conditions of enzyme in Ca-alginate beads were investigated and obtained with 2% alginate using 0.5mg/ml enzyme and 0.7M CaCl(2) solution. In order to prevent enzyme from leaking out of the gel beads, Ca-alginate beads were then coated with silicate. Enzyme loading efficiency and immobilization yield for silicate coated beads was determined as 98.1% and 71.27%, respectively and compared with non-coated ones which were 68.5% and 45.80%, respectively. Surface morphologies, structure and ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672241</comments>
            <pubDate>Tue, 31 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>The inhibitory effect of ethylenediamine on mushroom tyrosinase.</title>
            <link>http://www.medworm.com/index.php?rid=5672240&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22313842%26dopt%3DAbstract</link>
            <description>Authors: Alijanianzadeh M, Saboury AA, Ganjali MR, Hadi-Alijanvand H, Moosavi-Movahedi AA
    Abstract
    The inhibitory effect of ethylenediamine on both activities of mushroom tyrosinase (MT) at 20°C in a 10mM phosphate buffer solution (pH 6.8), was studied. l-DOPA and l-tyrosine were used as substrates of catecholase and cresolase activities, respectively. The results showed that ethylenediamine competitively inhibits both activities of the enzyme with inhibition constants (K(i)) of 0.18±0.05 and 0.14±0.01μM for catecholase and cresolase respectively, which are lower than the reported values for other MT inhibitors. For further insight a docking study between tyrosinase and ethylenediamine was performed. The docking simulation showed that ethylenediamine binds in the active site of...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672240</comments>
            <pubDate>Tue, 31 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672240</guid>        </item>
        <item>
            <title>Inverted binding due to a minor structural change in berberine enhances its phospholipase A(2) inhibitory effect.</title>
            <link>http://www.medworm.com/index.php?rid=5672250&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22305795%26dopt%3DAbstract</link>
            <description>This study brings out the significance of biotransformation in generation of better drug-lead compounds.
    PMID: 22305795 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672250</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672250</guid>        </item>
        <item>
            <title>An investigation on characteristics of rainbow trout coated using chitosan assisted with thyme essential oil.</title>
            <link>http://www.medworm.com/index.php?rid=5672248&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22305883%26dopt%3DAbstract</link>
            <description>Authors: Chamanara V, Shabanpour B, Gorgin S, Khomeiri M
    Abstract
    Our study aimed to determine the nutritional, textural and sensorial characteristics of butterfly-shaped rainbow trout which is coated by using enriched chitosan with thyme EO during 15 days of refrigerated storage (5±1°C). The treatments were Cs (chitosan; 2%, w/v), Cs+T (chitosan; 2%, w/v and Thymus vulgaris EO; 1%, v/v) and C (uncoated control samples). The composition of the EO was investigated by GC/MS. Generally, the EO was found to be rich in the active monoterpene phenols (thymol and carvacrol) and their corresponding monoterpene hydrocarbon precursors such as γ-terpinene and the oxygenated monoterpenes such as linalool. Nineteen constituent out of 116, representing 86.79% of the EO were identified, of whi...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672248</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672248</guid>        </item>
        <item>
            <title>In vitro antioxidant activities of the polysaccharides from Tricholoma lobayense.</title>
            <link>http://www.medworm.com/index.php?rid=5672247&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22305884%26dopt%3DAbstract</link>
            <description>Authors: Wang C, Chen Y, Hu M, Ding J, Xu C, Wang R
    Abstract
    The antioxidant activities of three polysaccharide components (TLH-1, TLH-2, TLH-3) extracted from Tricholoma lobayense were evaluated by three different in vitro methods, namely superoxide radical (O(2)(-)) scavenging activity, inhibition of mice erythrocyte hemolysis (MEH) and malondialdehyde (MDA) mediated by hydrogen peroxide (H(2)O(2)) and investigation of oxidative modification of human serum albumin (HSA) induced by 2,2-azobis(2-amidinopropane)dihydrochloride (AAPH) through fluorescence spectroscopy. The antioxidant experiments showed that the polysaccharides had a notable activity in scavenging O(2)(-) in a concentration-dependent manner; H(2)O(2)-induced MEH and formation of MDA were effectively inhibited; by flu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672247</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Silver nanoparticles/multiwalled carbon nanotube/polyaniline film for amperometric glutathione biosensor.</title>
            <link>http://www.medworm.com/index.php?rid=5672258&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22300999%26dopt%3DAbstract</link>
            <description>Authors: Narang J, Chauhan N, Jain P, Pundir CS
    Abstract
    A new silver nanoparticles (AgNPs)/carboxylated multiwalled carbon nanotubes (c-MWCNT)/polyaniline (PANI) film has been synthesized on Au electrode using electrochemical techniques. The enzyme glutathione oxidase (GSHOx) (EC 1.8.3.3) was immobilized covalently on the surface of AgNPs/c-MWCNT/PANI/Au electrode to construct the glutathione biosensor. The modified electrode was characterized by scanning electron microscopy (SEM), cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS) and Fourier transform infrared (FTIR) spectrophotometry. The biosensor showed optimum response within 4s at +0.4V vs. Ag/AgCl, pH 6.0 and 35°C, with a linear working range of 0.3-3500μM and a detection limit of 0.3μM. The glutathio...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672258</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672258</guid>        </item>
        <item>
            <title>Thermal stability and enzymatic activity of RNase A in the presence of cationic gemini surfactants.</title>
            <link>http://www.medworm.com/index.php?rid=5672257&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301000%26dopt%3DAbstract</link>
            <description>Authors: Amiri R, Bordbar AK, Laurents DV, Khosropour AR, Mohammadpoor-Baltork I
    Abstract
    The thermal stability and enzymatic activity of bovine pancreatic ribonuclease A (RNase A) have been investigated in the presence of a homologous series of cationic gemini surfactants (alkanediyl-α,ω-bis(hydroxyethyl methyl hexadecyl ammonium bromide)). UV, circular dichorism and fluorescence spectroscopies have been used for this study. The denaturation curves at various surfactant concentrations were analyzed on basis of a two-transition model to obtain values of T(m) (temperature at the midpoint of denaturation) and ΔH(m) (enthalpy change at T(m)) of each transition. The main conclusion of this study is that these cationic gemini surfactants slightly activate and stabilize RNase A below ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672257</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672257</guid>        </item>
        <item>
            <title>Modification of chitosan membrane with poly(vinyl alcohol) and biocompatibility evaluation.</title>
            <link>http://www.medworm.com/index.php?rid=5672256&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301001%26dopt%3DAbstract</link>
            <description>Authors: Zhuang PY, Li YL, Fan L, Lin J, Hu QL
    Abstract
    This work aimed to overcome chitosan (CS) membrane' drawbacks: mainly stiffness and hydrophobic surface by adding poly(vinyl alcohol) (PVA) and evaluate their biocompatibility. The chemical structure, crystalline and thermal properties were studied by FT-IR, XRD and DSC. The mechanical properties and wettability of CS/PVA membranes were studied by tensile test and static contact angle measurement. In vitro biocompatibility was also evaluated by MTS cytotoxicity assay and SEM examination. The results suggest that adding PVA into CS membrane could greatly improve CS membrane's flexibility and wettability. All the membranes prepared were biocompatible and have potential applications in GTR technology.
    PMID: 22301001 [PubMed -...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672256</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672256</guid>        </item>
        <item>
            <title>Anti-hepatoma activity in mice of a polysaccharide from the rhizome of Anemone raddeana.</title>
            <link>http://www.medworm.com/index.php?rid=5672255&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301002%26dopt%3DAbstract</link>
            <description>Authors: Liu Y, Li Y, Yang W, Zhang L, Cao G
    Abstract
    A neutral polysaccharide fraction (ARP) prepared from the rhizome of Anemone raddeana was tested for its anticancer activity in H22 tumor-bearing mice by oral administration. ARP could not only significantly inhibit the growth of H22 transplantable tumor, but also remarkably promote splenocytes proliferation, NK cell and CTL activity, as well as serum IL-2 and TNF-α production in tumor-bearing mice. In addition, ARP treatment to tumor bearing mice had no toxicity to body weight, the liver and kidney. Moreover it could reverse the hematological parameters induced by 5-fluorouracil (5-FU) to near normal. The above results suggested that the antitumor activity of ARP might be achieved by improving immune response, and they could a...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672255</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672255</guid>        </item>
        <item>
            <title>In vitro and in vivo evaluation of oridonin-loaded long circulating nanostructured lipid carriers.</title>
            <link>http://www.medworm.com/index.php?rid=5672253&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301003%26dopt%3DAbstract</link>
            <description>In conclusion, ORI-PEG-NLC could be a potential carrier to get prolonged retention time of oridonin in blood.
    PMID: 22301003 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672253</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672253</guid>        </item>
        <item>
            <title>Effect of PVA on the gel temperature of MC and release kinetics of KT from MC based ophthalmic formulations.</title>
            <link>http://www.medworm.com/index.php?rid=5672251&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22301004%26dopt%3DAbstract</link>
            <description>Authors: Bain MK, Bhowmick B, Maity D, Mondal D, Mollick MM, Paul BK, Bhowmik M, Rana D, Chattopadhyay D
    Abstract
    The effect of molecular weight of poly(vinyl alcohol) (PVA) and sodium chloride on the gelation temperature of methylcellulose (MC) was studied with the objective to develop a MC based formulation for sustained delivery of ketorolac tromethamine a model ophthalmic drug. Pure MC showed sol-gel transition at 61.2°C. In order to reduce the gelation temperature of MC and to increase the drug release time, PVA was used. Different techniques such as test tube tilting method, UV-vis spectroscopy, viscometry and rheometry were used to measure gelation temperature of all the binary combinations of MC and PVA. It was observed that the gelation temperature of MC was reduced with ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672251</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672251</guid>        </item>
        <item>
            <title>DNA template-assisted modulation of horseradish peroxidase activity.</title>
            <link>http://www.medworm.com/index.php?rid=5672249&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22305796%26dopt%3DAbstract</link>
            <description>Authors: Datta S, Dou X, Shibley A, Datta B
    Abstract
    The precise alignment of DNA molecules by Watson-Crick base-pairing combined with its polymeric characteristics have allowed DNA to be used as a template or scaffold for assembling materials. In this work, we investigate the role of calf-thymus DNA as a template for enhancing the horseradish peroxidase (HRP)-mediated oxidation of phenol and phenolic derivatives. The HRP-catalyzed oxidation of phenol into polyphenolic products and in presence of 4-aminoantipyrine into quinoneimine dye complexes is studied. Visible spectroscopy reveals an increased yield of both products of the enzymatic reaction in presence of calf-thymus DNA and is attributed to the prearrangement of the corresponding substrates on the DNA. The concentrations of ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5672249</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5672249</guid>        </item>
        <item>
            <title>Structure elucidation and antioxidant activity of a novel polysaccharide isolated from Boletus speciosus Forst.</title>
            <link>http://www.medworm.com/index.php?rid=5655094&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285986%26dopt%3DAbstract</link>
            <description>In this study, a novel heteropolysaccharide was isolated from the fruiting bodies of Boletus speciosus Forst through DEAE-cellulose column and Sephadex G-200 column. The Boletus speciosus Forst polysaccharide (BSFP-1) had a molecular weight of 1.33×10(4)Da and was mainly composed of l-Man and d-Gal which ratios were 2:1. Structural features of Boletus speciosus Forst polysaccharide (BSFP-1) were investigated by a combination of total hydrolysis, methylation analysis, gas chromatography-mass spectrometry (GC-MS), infrared (IR) spectra and nuclear magnetic resonance (NMR) spectroscopy. The results indicated that Boletus speciosus Forst polysaccharide (BSFP-1) had a backbone of (1→4)-α-l-mannopyranose residues which branches at O-6 based on the experimental results. The branches were main...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655094</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5655094</guid>        </item>
        <item>
            <title>Evaluation of immobilized lipases on poly-hydroxybutyrate beads to catalyze biodiesel synthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5655093&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285987%26dopt%3DAbstract</link>
            <description>Authors: Mendes AA, Oliveira PC, Vélez AM, Giordano RC, Giordano RD, de Castro HF
    Abstract
    Five microbial lipase preparations from several sources were immobilized by hydrophobic adsorption on small or large poly-hydroxybutyrate (PHB) beads and the effect of the support particle size on the biocatalyst activity was assessed in the hydrolysis of olive oil, esterification of butyric acid with butanol and transesterification of babassu oil (Orbignya sp.) with ethanol. The catalytic activity of the immobilized lipases in both olive oil hydrolysis and biodiesel synthesis was influenced by the particle size of PHB and lipase source. In the esterification reaction such influence was not observed. Geobacillus thermocatenulatus lipase (BTL2) was considered to be inadequate to catalyze biod...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655093</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthase.</title>
            <link>http://www.medworm.com/index.php?rid=5655092&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285988%26dopt%3DAbstract</link>
            <description>Authors: Ahmad Z, Ahmad M, Okafor F, Jones J, Abunameh AM, Cheniya RK, Kady IO
    Abstract
    In this paper we present the inhibitory effect of a variety of structurally modulated/modified polyphenolic compounds on purified F(1) or membrane bound F(1)F(o)Escherichia coli ATP synthase. Structural modulation of polyphenols with two phenolic rings inhibited ATP synthase essentially completely; one or three ringed polyphenols individually or fused together inhibited partially. We found that the position of hydroxyl and nitro groups plays critical role in the degree of binding and inhibition of ATPase activity. The extended positioning of hydroxyl groups on imino diphenolic compounds diminished the inhibition and abridged position enhanced the inhibition potency. This was contrary to the effe...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655092</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>A new chitosan-thymine conjugate: Synthesis, characterization and biological activity.</title>
            <link>http://www.medworm.com/index.php?rid=5655096&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285484%26dopt%3DAbstract</link>
            <description>Authors: Kumar S, Koh J, Kim H, Gupta MK, Dutta PK
    Abstract
    Conjugation of chitosan with nucleobases is expected to expand its not only antimicrobial activity but also anti-cancer activity. Here, we report the synthesis of a novel chitosan-thymine conjugate by the reaction between chitosan and thymine-1-yl-acetic acid followed by acylation. The synthesized conjugate was characterized by FTIR, XRD, (1)H NMR, TGA and SEM. The microbiological screening results demonstrated the antimicrobial activity of the conjugate against bacteria viz., Escherichia coli, Staphylococcus aureus, and fungi viz., Aspergillus niger. The chitosan-thymine conjugate also inhibited (p&amp;lt;0.05) the proliferation of human liver cancer cells (HepG2) in a dose-dependent manner but had no cellular toxicity in non...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655096</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>A new proposed sweet potato starch granule structure-Pomegranate concept.</title>
            <link>http://www.medworm.com/index.php?rid=5655095&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285985%26dopt%3DAbstract</link>
            <description>Authors: Xijun L, Lin L, Kunsheng Z, Ying X, Jiaxin L
    Abstract
    There are two competing concepts about organization of starch granule, fibrillar concept (or amylopectin clustering concept) and blocklet concept. A new micrograph of gelatinized sweet potato starch mixed with lactose might combine the two concepts and recover the mysterious structure of starch granule. Here we propose a possible granule structure of sweet potato starch by analyzing its gelatinization micrographs mixed with different carbohydrates. As the structure of pomegranate, out-layer of granule is equivalent to skin of pomegranate, blocklets are same to garnet of pomegranate, the amylopectin clusters with one reducing end at hilum, equivalent to primary body of pomegranate, constitute the basic structure of granu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655095</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>The contribution of side chains to antitumor activity of a polysaccharide from Codonopsis pilosula.</title>
            <link>http://www.medworm.com/index.php?rid=5655091&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285989%26dopt%3DAbstract</link>
            <description>Authors: Xu C, Liu Y, Yuan G, Guan M
    Abstract
    In order to assess the potential contribution of the side chains of a polysaccharide (CPPW1) from the roots of Codonopsis pilosula to the biological activities, we chose CPPW1 and its backbone (CPPW1B) as the research targets to compare them with their antitumor and immunomodulatory activity. The results demonstrated CPPW1 could significantly inhibit the tumor growth of H22-bearing mice and simulate lymphocyte proliferation. Meanwhile the phagocytic capability of macrophages and NO production were also enhanced. However, CPPW1B could only inhibit the tumor weight and did not work to immune system at all. Additionally, both CPPW1 and CPPW1B had no toxicity in vivo. Taken together with all data, we found the sugar side chains attached to ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655091</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5655091</guid>        </item>
        <item>
            <title>Molecular characterization of a novel trehalose-6-phosphate hydrolase, TreA, from Bacillus licheniformis.</title>
            <link>http://www.medworm.com/index.php?rid=5655090&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285990%26dopt%3DAbstract</link>
            <description>Authors: Chuang TT, Ong PL, Wang TF, Huang HB, Chi MC, Lin LL
    Abstract
    An unidentified Bacillus licheniformis trehalose-6-phosphate hydrolase (BlTreA) gene was cloned and heterologously expressed in Escherichia coli M15 cells. The over-expressed BlTreA was purified to apparent homogeneity by metal-affinity chromatography and its molecular mass was determined to be approximately 65.9kDa. The temperature and pH optima for BlTreA were 30°C and 8.0, respectively. The enzyme hydrolyzed p-nitrophenyl-α-d-glucopyranoside (pNPG) and trehalose-6-phosphate efficiently, but it was inactive toward five other p-nitrophenyl derivatives. Steady-state kinetics with pNPG showed that BlTreA had a K(M) value of 5.2mM and a k(cat) value of 30.2s(-1). Circular dichroism analysis revealed that the sec...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5655090</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5655090</guid>        </item>
        <item>
            <title>Preparation and characterization of silica gel/chitosan composite for the removal of Cu(II) and Pb(II).</title>
            <link>http://www.medworm.com/index.php?rid=5636840&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22281115%26dopt%3DAbstract</link>
            <description>Authors: Rajiv Gandhi M, Meenakshi S
    Abstract
    Silica gel/chitosan composite (SiCS) was prepared via., sol-gel method by mixing silica gel and chitosan and cross-linked with bifunctional cross-linker glutaraldhyde. The SiCS composite was characterized using FT-IR, SEM-EDAX, XRD and BET methods. The sorption of copper and lead ions onto SiCS has been investigated. The SiCS composite was found to have excellent metal sorption capacity than the silica gel (Si) and chitosan (CS). The sorption experiments were carried out in batch mode to optimize various parameters viz., contact time, pH, initial metal ion concentration, co-ions and temperature that influence the sorption. Langmuir, Freundlich and Dubinin-Radushkevich adsorption isotherm models were applied to describe isotherm constant...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636840</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636840</guid>        </item>
        <item>
            <title>Co-solvent mediated thermal stabilization of chondroitinase ABC I form Proteus vulgaris.</title>
            <link>http://www.medworm.com/index.php?rid=5636841&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22274395%26dopt%3DAbstract</link>
            <description>This study has been undertaken to determine the effects of glycerol, sorbitol and trehalose on cABC I activity and thermal stability. The results indicated that the enzyme catalytic activity and intrinsic fluorescence intensity increased in the presence of these cosolvents whereas no considerable conformational changes observed in far-UV CD spectra. Thermal CD experiment revealed an increase in T(m) of cABC I in the presence of cosolvents which was significant for trehalose. Our results support the idea that cABC I has stabilized in the presence of glycerol, sorbitol and trehalose. Therefore, the use of these cosolvents seems to be promising for improvement in shelf-life and clinical applications of this drug enzyme.
    PMID: 22274395 [PubMed - as supplied by publisher] (Source: Internati...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636841</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636841</guid>        </item>
        <item>
            <title>Silica-encapsulated magnetic nanoparticles: Enzyme immobilization and cytotoxic study.</title>
            <link>http://www.medworm.com/index.php?rid=5636843&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22269345%26dopt%3DAbstract</link>
            <description>Authors: Ashtari K, Khajeh K, Fasihi J, Ashtari P, Ramazani A, Vali H
    Abstract
    Silica-encapsulated magnetic nanoparticles (MNPs) were prepared via microemulsion method. The products were characterized by high resolution transmission electron microscopy (HRTEM) and energy-dispersive X-ray spectrum (EDS). MNPs with no observed cytotoxic activity against human lung carcinoma cell and brine shrimp lethality were used as suitable support for glucose oxidase (GOD) immobilization. Binding of GOD onto the support was confirmed by the FTIR spectra. The amount of immobilized GODs was 95mg/g. Storage stability study showed that the immobilized GOD retained 98% of its initial activity after 45 days and 90% of the activity was also remained after 12 repeated uses. Considerable enhancements in t...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636843</comments>
            <pubDate>Mon, 16 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636843</guid>        </item>
        <item>
            <title>Preparation, characterization and anticoagulant activity in vitro of heparin-like 6-carboxylchitin derivative.</title>
            <link>http://www.medworm.com/index.php?rid=5636846&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266383%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Cai J, Wu K, Li D, Hu Y, Li G, Du Y
    Abstract
    A series of heparin-like 6-carboxylchitin derivatives with different N-acetyl group and sulfate group contents were prepared. Their structures were characterized by element analysis, FT-IR, (13)C NMR, and gel permeation chromatography. Their anticoagulant activity in vitro was investigated for human plasma with respect to activated partial thromboplastin time (APTT). The results showed all 6-carboxylchitin derivatives prolonged APTT within the scope of studied degree of sulfation (0.28-1.03) and Mws (4.3-13.7kDa). Their anticoagulant activity strongly depended on their structures. 3,6-O-sulfated group promoted the anticoagulant activity. Only incorporation of N-sulfated group into deacetylated 6-carboxylchitin could not ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636846</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636846</guid>        </item>
        <item>
            <title>Structure and antimicrobial activities of benzoyl phenyl-thiosemicarbazone-chitosans.</title>
            <link>http://www.medworm.com/index.php?rid=5636845&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266384%26dopt%3DAbstract</link>
            <description>Authors: Zhong Z, Aotegen B, Xu H, Zhao S
    Abstract
    Previously, we had prepared acetyl phenyl-thiosemicarbazone derivatives of chitosan, and their antimicrobial activities were analyzed. The purpose of the present study was to further assess the relationship between the structure and antimicrobial activities of benzoyl phenyl-thiosemicarbazone-chitosan. Ten new benzoyl phenyl-thiosemicarbazone-chitosans were prepared and their structures were characterized by FT-IR and elemental analysis. The antimicrobial experiment against four species of bacteria and four crop-threatening pathogenic fungi were conducted based on the derivatives of chitosan with different molecular weight at different concentrations. The results indicated that the antimicrobial activities of benzoyl phenyl-thiosem...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636845</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636845</guid>        </item>
        <item>
            <title>Variations in the molecular masses of the capsular exopolysaccharides amylovoran, pyrifolan and stewartan.</title>
            <link>http://www.medworm.com/index.php?rid=5636844&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266385%26dopt%3DAbstract</link>
            <description>Authors: Schollmeyer M, Langlotz C, Huber A, Coplin DL, Geider K
    Abstract
    Erwinia amylovora, causing fire blight of apple, pear and some ornamentals, Erwinia pyrifoliae, causing Asian pear blight, and Pantoea stewartii, causing Stewart's wilt of sweet maize, synthesize capsular extracellular polysaccharides (EPSs) with a high molecular mass. The EPSs are virulence factors and form viscous aggregates, which participate in clogging vessels of infected plants and causing wilting. The sizes of EPSs produced under different environmental growth conditions were determined by analysis with large pore HPLC columns. Their molecular mass of ca. 5MDa, when isolated from agar plates, decreases to ca. 1MDa for E. amylovora amylovoran from freeze-dried supernatants from liquid cultures and to 2M...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636844</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636844</guid>        </item>
        <item>
            <title>Biocomposite films based on alginate and organically modified clay.</title>
            <link>http://www.medworm.com/index.php?rid=5636842&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22269346%26dopt%3DAbstract</link>
            <description>Authors: Tezcan F, Günister E, Ozen G, Erim FB
    Abstract
    Sodium alginate/sodium montmorillonite hybrid films were prepared by casting from the suspension of sodium alginate and different clay samples. Clay samples had been modified with a cationic surfactant, a cationic polymer, and a small polar molecule, respectively. Benzethonium chloride, polyethyleneimine and urea were used as clay modifiers. The composite films begin to disintegrate at a higher temperature and with less weight loss than the pure alginate films. This suggests an enhancement of the film thermal stability due to the modification of the alginate with clay samples.
    PMID: 22269346 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636842</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636842</guid>        </item>
        <item>
            <title>Synthesis and characterization of a novel potato starch derivative with cationic acetylcholine groups.</title>
            <link>http://www.medworm.com/index.php?rid=5636848&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266328%26dopt%3DAbstract</link>
            <description>Authors: Zhang B, Ni B, Lü S, Cui D, Liu M, Gong H, Han F
    Abstract
    A novel substance, cationic acetylcholine potato starch (CAPS), was developed for the first time. The synthesis process had three steps: first, carboxymethyl potato starch (CMPS) was synthesized under sodium hydroxide alkaline condition and in isopropyl alcohol organic media; second, bromocholine chloride (BCC) was synthesized with sulphuric acid as a catalytic agent; finally, CAPS was synthesized by the reaction of CMPS with BCC in N,N'-dimethylformamide (DMF). The degree of substitution (DS) of CAPS was determined by ammonia gas-sensing electrode and elemental analysis. CAPS was characterized by Fourier transformed infrared (FTIR) and near infrared (FTNIR) spectroscopy, scanning electron microscopy (SEM), X-ray d...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636848</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636848</guid>        </item>
        <item>
            <title>Adjuvanticity of compound polysaccharides on chickens against Newcastle disease and avian influenza vaccine.</title>
            <link>http://www.medworm.com/index.php?rid=5636847&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266329%26dopt%3DAbstract</link>
            <description>In conclusion, appropriate dose of APS-sEPS may be a safe and efficacious immune stimulator candidate suitable for vaccines.
    PMID: 22266329 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636847</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636847</guid>        </item>
        <item>
            <title>Spectroscopic investigation of collagen scaffolds impregnated with AgNPs coated by PEG/TX-100 mixed systems.</title>
            <link>http://www.medworm.com/index.php?rid=5619096&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22260903%26dopt%3DAbstract</link>
            <description>Authors: Mandal A, Meda V, Zhang WJ, Dalai AK
    Abstract
    Silver nanoparticles have received attention as novel antimicrobial agents due to their high surface area to volume ratio and the unique chemical and physical properties. In order to study the effects of capping agents on silver nanoparticles (AgNPs), the nanoparticles were synthesized via chemical reduction method using different concentrations (0.3mM, 0.6mM and 0.9mM) of polyethylene glycol (PEG) and Triton X-100 (TX). Also, AgNPs capped by the combinations of both PEG and TX were synthesized. These coated AgNPs were incorporated into collagen, lyophilized to form scaffolds and characterized by FTIR and FT-Raman spectroscopy. Results on mechanical property of all the scaffolds displayed no significant difference in the percen...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619096</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619096</guid>        </item>
        <item>
            <title>Evidence regarding the hypothesis that the histidine-histidine contact pairs may affect protein stability.</title>
            <link>http://www.medworm.com/index.php?rid=5619097&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22257446%26dopt%3DAbstract</link>
            <description>Authors: Haghani K, Khajeh K, Naderi-Manesh H, Ranjbar B
    Abstract
    It has been lately proposed that the interaction between like-charged residues stabilizes the native state of proteins. To explore this, we created a histidine-histidine pair in the Ca-III binding site of the Bacillus amyloliquefaciens α-amylase (BAA) and then examined the impact of this pairing on the BAA. For this purpose, we used site-directed mutagenesis (SDM) to substitute Pro407 with His, Ala, Gln, Arg, and Glu in the BAA. Subsequently, thermostability, kinetic parameters and structural properties of these variants were measured. Moreover, His-His pairing effect on the BAA thermostability was examined by simultaneous mutation of two residues (P407H/H406A and P407H/H406N). The data exhibited a significant impro...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619097</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619097</guid>        </item>
        <item>
            <title>Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose.</title>
            <link>http://www.medworm.com/index.php?rid=5619098&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22245359%26dopt%3DAbstract</link>
            <description>Authors: Hu WJ, Yan L, Park D, Jeong HO, Chung HY, Yang JM, Yin SJ, Qian GY
    Abstract
    Tyrosinase plays a central role in biological pigment formation, and hence knowledge of tyrosinase catalytic mechanisms and regulation may have medical, cosmetic, and agricultural applications. We found in this study that arabinose significantly inhibited tyrosinase, and this was accompanied by conformational changes in enzyme structure. Kinetic analysis showed that arabinose-mediated inactivation followed first-order kinetics, and single and multiple classes of rate constants were measured. Arabinose displayed a mixed-type inhibitory mechanism with K(i)=0.22±0.07mM. Measurements of intrinsic and ANS-binding fluorescence showed that arabinose induced tyrosinase to unfold and expose inner hydrophob...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619098</comments>
            <pubDate>Sun, 08 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619098</guid>        </item>
        <item>
            <title>Antioxidant activities potential of tea polysaccharide fractions obtained by ultra filtration.</title>
            <link>http://www.medworm.com/index.php?rid=5595359&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230610%26dopt%3DAbstract</link>
            <description>Authors: Wang Y, Yang Z, Wei X
    Abstract
    Three polysaccharide fractions (TPS1, TPS2 and TPS3) with different molecular weights were obtained using ultra filtration membranes from crude tea polysaccharide (CTPS) extracted from abandoned lower grade tea leaves. Each fraction contained different contents of neutral sugar, uronic acid, protein, and total polyphenols. These differences provided basis for the antioxidant and free radical scavenging activity of these polysaccharide fractions. The molecular weights of TPS1, TPS2, and TPS3 were around 2.40×10(5)Da, 2.14×10(4)Da, and 2.46×10(3)Da, respectively. In general, TPS1 and CTPS had stronger antioxidant activity, TPS2 and TPS3 had lower antioxidant activity. TPS1 had higher activity for DPPH and lipid per oxidation inhibition. But ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595359</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595359</guid>        </item>
        <item>
            <title>Design and characterization of antitumor drug paclitaxel-loaded chitosan nanoparticles by W/O emulsions.</title>
            <link>http://www.medworm.com/index.php?rid=5595358&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230611%26dopt%3DAbstract</link>
            <description>Authors: Xu J, Ma L, Liu Y, Xu F, Nie J, Ma G
    Abstract
    Chitosan nanoparticles and paclitaxel loaded chitosan nanoparticles were prepared by emulsification-crosslinking method in a W/O emulsion system, using glutaraldehyde as crosslinking agent. The mean diameter of chitosan nanoparticles decreased with increase of pH value of the reaction system from 4.5 to 6.5, and increased when the pH exceeded 6.5. Ultraviolet spectrum analysis showed that the largest loading efficiency and encapsulation efficiency could be 8.55% and 94.01%, respectively. In vitro drug release profile was also determined by ultraviolet spectrometry. MTT assays revealed that the blank chitosan nanoparticles had almost none toxicity, and cell culture was carried out accordingly.
    PMID: 22230611 [PubMed - as sup...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595358</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595358</guid>        </item>
        <item>
            <title>Immobilization of β-d-galactosidase from Kluyveromyces lactis on functionalized silicon dioxide nanoparticles: Characterization and lactose hydrolysis.</title>
            <link>http://www.medworm.com/index.php?rid=5595357&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230612%26dopt%3DAbstract</link>
            <description>Authors: Verma ML, Barrow CJ, Kennedy JF, Puri M
    Abstract
    β-d-Galactosidase (BGAL) from Kluyveromyces lactis was covalently immobilized to functionalized silicon dioxide nanoparticles (10-20nm). The binding of the enzyme to the nanoparticles was confirmed by Fourier transform-infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). Functionalized nanoparticles showed 87% immobilization yield. Soluble and immobilized enzyme preparation exhibited pH-optima at pH 6.5 and 7.0, respectively, with temperature optima at 35 and 40°C, respectively. Michaelis constant (K(m)) was 4.77 and 8.4mM for free and immobilized BGAL, respectively. V(max) for the soluble and immobilized enzyme was 12.25 and 13.51U/ml, respectively. Nanoparticle immobilized BGAL demonstrated improved stabi...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595357</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595357</guid>        </item>
        <item>
            <title>Potential biosorbent based on sugarcane bagasse modified with tetraethylenepentamine for removal of eosin Y.</title>
            <link>http://www.medworm.com/index.php?rid=5595356&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22230613%26dopt%3DAbstract</link>
            <description>Authors: Jiang GB, Lin ZT, Huang XY, Zheng YQ, Ren CC, Huang CK, Huang ZJ
    Abstract
    Tetraethylenepentamine (TEPA) modified sugarcane bagasse (SB), a novel biosorbent (TEPA-MSB), was proved to be an effective adsorbent for anionic dyes due to the introduced functional amino groups. FTIR, TG and DSC analysis were employed to characterize the sorbent. The effects of pH, temperature, contact time and initial concentration of dye on the adsorption of eosin Y were investigated. The experimental data fit very well to the Langmuir model, giving a maximum sorption capacity of 399.04mg/g at 25°C. And the kinetic data were well described by the pseudo-second-order kinetic model. pH 6 was the optimal pH for eosin Y adsorption, and the maximum adsorption capacity of TEPA-MSB calculated by Langm...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595356</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595356</guid>        </item>
        <item>
            <title>Preparation and characterization of chitosan-carbon nanotube scaffolds for bone tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5595355&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234296%26dopt%3DAbstract</link>
            <description>In this study, we have prepared scaffolds with the use of low and high molecular weight chitosan with 0.0025%, 0.005% and 0.01% weight of f-multiwalled carbon nanotube (f-MWCNT) by freezing and lyophilization method and physiochemically characterized as bone graft substitutes. Fourier Transform Infrared Spectroscopy, X-Ray Diffraction Analysis, Thermal Gravimetric Analysis, Scanning Electron Microscopy and Optical Microscopy results indicated that the f-MWCNT was uniformly dispersed in chitosan matrix and there was a chemical interaction between chitosan and f-MWCNT. The water uptake ability and porosity of scaffolds increased with an increase the amount of f-MWCNT. The cell proliferation, protein content, alkaline phosphatase and mineralization of the composite scaffolds were higher than ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595355</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595355</guid>        </item>
        <item>
            <title>Presence of alternating glucosaminoglucan in the sheath of Thiothrix nivea.</title>
            <link>http://www.medworm.com/index.php?rid=5526197&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085752%26dopt%3DAbstract</link>
            <description>Authors: Takeda M, Kondo K, Yamada M, Sumikawa M, Koizumi J, Mashima T, Katahira M
    Abstract
    A sheath-forming sulfa oxidizer, Thiothrix nivea, was mixotrophically cultured in a medium supplemented with acetic acid and sodium disulfide. Its sheath, a microtube-like extracellular supermolecule, was prepared by selectively removing the cells with lysozyme, sodium dodecyl sulfate, and sodium hydroxide. The sheath was not visibly affected by hydrazine treatment, suggesting that it is not a proteinous supermolecule. From the acid hydrolysate of the sheath, glucose and glucosamine were detected in an approximate molar ratio of 1:1. Three other saccharic compounds were detected and recovered by HPLC as fluorescent derivatives prepared by reaction with 4-aminobenzoic acid ethyl ester. Nuclea...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526197</comments>
            <pubDate>Thu, 22 Dec 2011 09:59:28 +0100</pubDate>
            <guid isPermaLink="false">5526197</guid>        </item>
        <item>
            <title>Structures and anti-HSV-2 activities of neutral polysaccharides from an edible plant, Basella rubra L.</title>
            <link>http://www.medworm.com/index.php?rid=5526196&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085753%26dopt%3DAbstract</link>
            <description>Authors: Dong CX, Hayashi K, Mizukoshi Y, Lee JB, Hayashi T
    Abstract
    Four neutral polysaccharides (BRN-1, BRN-2, BRN-3 and BRN-4) were isolated from the hot water extract of the aerial part of Basella rubra L. They were found to consist of a large amount of d-galactose (81.0-92.4%) and small amounts of l-arabinose (5.4-7.8%), d-glucose (2.2-11.0%) and mannose (∼2.9%). Linkage analysis revealed that all these neutral polysaccharides might be arabinogalactan type I polysaccharides in different molecular weight and chain length. Among them, only BRN-3 showed antiviral activity against herpes simplex virus type 2 (HSV-2) with 50% inhibitory concentration of 55μg/mL without showing the cytotoxicity up to 2300μg/mL. Furthermore, the main antiviral target of BRN-3 was shown to be the ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526196</comments>
            <pubDate>Thu, 22 Dec 2011 09:59:19 +0100</pubDate>
            <guid isPermaLink="false">5526196</guid>        </item>
        <item>
            <title>Antioxidant activities of polysaccharides from Lentinus edodes and their significance for disease prevention.</title>
            <link>http://www.medworm.com/index.php?rid=5526190&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085754%26dopt%3DAbstract</link>
            <description>In this study, their chemical and physical characteristics of polysaccharide fractions and antioxidant capacities, including scavenging activity against hydroxyl radicals, superoxide radicals and Fe(2+)-chelating ability, were valuated. The results showed that LEPC1 exhibited significantly antioxidant activity at a concentration-dependent manner. Therefore these results indicated that the water-extractable polysaccharide fraction was a potent antioxidant and could be developed to be new health medicine for fighting against various human diseases.
    PMID: 22085754 [PubMed - in process] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526190</comments>
            <pubDate>Thu, 22 Dec 2011 09:59:09 +0100</pubDate>
            <guid isPermaLink="false">5526190</guid>        </item>
        <item>
            <title>How does sucrose stabilize the native state of globular proteins?</title>
            <link>http://www.medworm.com/index.php?rid=5526189&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085755%26dopt%3DAbstract</link>
            <description>Authors: Graziano G
    Abstract
    It is well known that sucrose stabilizes the native state of globular proteins against both chemical denaturants and temperature. A largely accepted explanation of sucrose-induced stabilization is not yet emerged. It is shown that the same theoretical approach able to rationalize the occurrence of cold denaturation, the contrasting role of GdmCl and Gdm(2)SO(4), and the TMAO counteraction of urea denaturing activity [PCCP 12 (2010) 14245; PCCP 13 (2011) 12008; PCCP 13 (2011) 17689] works well also in the case of sucrose. The solvent-excluded volume effect plays the fundamental role because sucrose addition to water causes a marked increase in volume packing density due to the large size of sucrose molecules, that act as crowding agents.
    PMID: 220857...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526189</comments>
            <pubDate>Thu, 22 Dec 2011 09:58:59 +0100</pubDate>
            <guid isPermaLink="false">5526189</guid>        </item>
        <item>
            <title>Characterization and application of a detergent-stable alkaline α-amylase from Bacillus subtilis strain AS-S01a.</title>
            <link>http://www.medworm.com/index.php?rid=5526187&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085756%26dopt%3DAbstract</link>
            <description>Authors: Roy JK, Rai SK, Mukherjee AK
    Abstract
    A strain AS-S01a, capable of producing high-titer alkaline α-amylase, was isolated from a soil sample of Assam, India and was taxonomically identified as Bacillus subtilis strain AS-S01a. Optimized α-amylase yield by response surface method (RSM) was obtained as 799.0U with a specific activity of 201.0U/mg in a process control bioreactor. A 21.0kDa alkaline α-amylase purified from this strain showed optimum activity at 55°C and pH 9.0, and it produced high molecular weight oligosaccharides including small amount of glucose from starch as the end product. The K(m) and V(max) values for this enzyme towards starch were determined as 1.9mg/ml and 198.21μmol/min/mg, respectively. The purified α-amylase retained its activity in presenc...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526187</comments>
            <pubDate>Thu, 22 Dec 2011 09:58:49 +0100</pubDate>
            <guid isPermaLink="false">5526187</guid>        </item>
        <item>
            <title>Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study.</title>
            <link>http://www.medworm.com/index.php?rid=5526186&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22093614%26dopt%3DAbstract</link>
            <description>Authors: Si YX, Wang ZJ, Park D, Chung HY, Wang SF, Yan L, Yang JM, Qian GY, Yin SJ, Park YD
    Abstract
    Tyrosinase inhibitors have potential applications in medicine, cosmetics and agriculture to prevent hyperpigmentation or browning effects. Some of the flavonoids mostly found in herbal plants and fruits are revealed as tyrosinase inhibitors. We studied the inhibitory effects of one such flavonoid, hesperetin, on mushroom tyrosinase using inhibition kinetics and computational simulation. Hesperetin reversibly inhibited tyrosinase in a competitive manner with K(i)=4.03±0.26mM. Measurements of ANS-binding fluorescence showed that hesperetin induced the hydrophobic disruption of tyrosinase. For further insight, we used the docking algorithms to simulate binding between tyrosinase and ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526186</comments>
            <pubDate>Thu, 22 Dec 2011 09:58:39 +0100</pubDate>
            <guid isPermaLink="false">5526186</guid>        </item>
        <item>
            <title>Corn porous starch: Preparation, characterization and adsorption property.</title>
            <link>http://www.medworm.com/index.php?rid=5526184&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100869%26dopt%3DAbstract</link>
            <description>This study was carried out to develop a new type of modified starch based on α-amylase and glucoamylase. The structural and chemical characteristics of the porous starch were determined by Fourier-transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), X-ray diffraction (XRD) and differential scanning calorimetry (DSC). The potential application of the porous starch as an adsorbent was evaluated using methyl violet as an adsorbed model. The adsorption capacity was optimized by investigating the reaction factors, including the mass ratio of α-amylase to glucoamylase (m(α-amylase)/m(glucoamylase)), the mass ratio of total amount of enzymes to starch (m(enzyme)/m(St)), the ratio of liquid volume to starch mass ( [Formula: see text] ), pH value of the reaction solution, ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526184</comments>
            <pubDate>Thu, 22 Dec 2011 09:58:19 +0100</pubDate>
            <guid isPermaLink="false">5526184</guid>        </item>
        <item>
            <title>Antifungal property of quaternized chitosan and its derivatives.</title>
            <link>http://www.medworm.com/index.php?rid=5526183&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100980%26dopt%3DAbstract</link>
            <description>Authors: Sajomsang W, Gonil P, Saesoo S, Ovatlarnporn C
    Abstract
    Five water-soluble chitosan derivatives were carried out by quaternizing either iodomethane or N-(3-chloro-2-hydroxypropyl) trimethylammonium chloride (Quat188) as a quaternizing agent under basic condition. The degree of quaternization (DQ) ranged between 28±2% and 90±2%. The antifungal activity was evaluated by using disc diffusion method, minimum inhibitory concentration (MIC) and minimum fungicidal concentration (MFC) methods against Trichophyton rubrum (T. rubrum), Trichophyton mentagrophyte (T. mentagrophyte), and Microsporum gypseum (M. gypseum) at pH 7.2. All quaternized chitosans and its derivatives showed more effective against T. rubrum than M. gypseum and T. mentagrophyte. The MIC and MFC values were fou...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526183</comments>
            <pubDate>Thu, 22 Dec 2011 09:58:09 +0100</pubDate>
            <guid isPermaLink="false">5526183</guid>        </item>
        <item>
            <title>Synthesis and antihyperlipidemic activity of acetylated derivative of ulvan from Ulva pertusa.</title>
            <link>http://www.medworm.com/index.php?rid=5526181&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22115715%26dopt%3DAbstract</link>
            <description>In this study, acetylated ulvan (AU) was prepared with acetic anhydride in N,N-dimethylacetamide, and the antihyperlipidemic activity of natural ulvan and its acetylated ulvan derivative (AU) in mice was determined. Obvious differences in antihyperlipidemic activity between natural ulvan and its derivative were observed, moreover, AU showed stronger antihyperlipidemic activity on triglyceride (TG) and low density lipoprotein cholesterol (LDL-C).
    PMID: 22115715 [PubMed - in process] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526181</comments>
            <pubDate>Thu, 22 Dec 2011 09:57:48 +0100</pubDate>
            <guid isPermaLink="false">5526181</guid>        </item>
        <item>
            <title>Application of reactive salicylanilide to viscose fabrics as antibacterial and antifungus finishing.</title>
            <link>http://www.medworm.com/index.php?rid=5526180&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22115716%26dopt%3DAbstract</link>
            <description>Authors: Atef El-Sayed A, Dorgham SM, Kantouch A
    Abstract
    In the present study salicylanilide was reacted with 2,4,6-trichloro-1,3,5-triazine producing reactive salicylanilide at a yield of 45% according to reaction conditions set. The reactive salicylanilide was confirmed structurally through FT-IR analysis. Pristine viscose fabric was treated with active salicylanilide to impart permanent antibacterial and antifungus properties to the fabric. Covalently attached reactive salicylanilide, as revealed, was quantitatively assessed through spectrophotometric and nitrogen elemental analysis. The antibacterial and antifungus capability of reactive salicylanilide treated viscose fabric; fastness and washing reproduction were examined and evaluated.
    PMID: 22115716 [PubMed - in process...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526180</comments>
            <pubDate>Thu, 22 Dec 2011 09:57:37 +0100</pubDate>
            <guid isPermaLink="false">5526180</guid>        </item>
        <item>
            <title>Investigation of the inclusion behavior of chlorogenic acid with hydroxypropyl-β-cyclodextrin.</title>
            <link>http://www.medworm.com/index.php?rid=5526178&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22115718%26dopt%3DAbstract</link>
            <description>Authors: Chao J, Wang H, Zhao W, Zhang M, Zhang L
    Abstract
    The inclusion complexation behavior of chlorogenic acid (CGA) with the hydroxypropyl-β-cyclodextrin (HP-β-CD) was investigated in both solution and the solid state by UV-vis and fluorescence spectroscopy, infrared spectroscopy (IR), NMR spectroscopy as well as differential scanning calorimetry (DSC). The experimental results indicate that CGA is able to form an inclusion complex with HP-β-CD. The inclusion complex has a stoichiometry of 1:1 and the formation constant was calculated to be 155.7M(-1). The antioxidant activity of CGA on complexation with HP-β-CD increased as compared to uncomplexed CGA. NMR spectroscopic studies show that the aromatic ring and the vinyl group of CGA are deeply included inside the CD cavity...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526178</comments>
            <pubDate>Thu, 22 Dec 2011 09:57:16 +0100</pubDate>
            <guid isPermaLink="false">5526178</guid>        </item>
        <item>
            <title>Homology models of four Agaricus bisporus tyrosinases.</title>
            <link>http://www.medworm.com/index.php?rid=5526177&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22119959%26dopt%3DAbstract</link>
            <description>Authors: Inlow JK
    Abstract
    Partially purified tyrosinase from the white button mushroom Agaricus bisporus is available commercially and is a widely used experimental model for the study of tyrosinase. The structure of an H(2)L(2) tetrameric form of the mushroom enzyme was recently determined by X-ray crystallography. In this structure the two H subunits originate from the PPO3 gene, and the two L subunits are formed by a protein of unknown function with a lectin-like fold. However, the X-ray structures and oligomeric states of the mushroom PPO1, PPO2, PPO4, and PPO5 gene products remain unknown. Commercial mushroom tyrosinase powder is a mixture containing several or all of these tyrosinases, so knowledge of their structures should provide insight regarding interpretation of experi...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526177</comments>
            <pubDate>Thu, 22 Dec 2011 09:57:06 +0100</pubDate>
            <guid isPermaLink="false">5526177</guid>        </item>
        <item>
            <title>Bio-composite scaffolds containing chitosan/nano-hydroxyapatite/nano-copper-zinc for bone tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5526174&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22123094%26dopt%3DAbstract</link>
            <description>Authors: Tripathi A, Saravanan S, Pattnaik S, Moorthi A, Partridge NC, Selvamurugan N
    Abstract
    The current study involves fabrication and characterization of bio-composite scaffolds containing chitosan (CS), nano-hydroxyapatite (nHAp) and Cu-Zn alloy nanoparticles (nCu-Zn) by freeze drying technique. The fabricated composite scaffolds (CS/nHAp and CS/nHAp/nCu-Zn) were characterized by SEM, EDX, XRD and FT-IR studies. The addition of nCu-Zn in the CS/nHAp scaffolds significantly increased swelling, decreased degradation, increased protein adsorption, and increased antibacterial activity. The CS/nHAp/nCu-Zn scaffolds had no toxicity towards rat osteoprogenitor cells. So the developed CS/nHAp/nCu-Zn scaffolds have advantageous and potential applications over the CS-nHAp scaffolds for ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526174</comments>
            <pubDate>Thu, 22 Dec 2011 09:56:36 +0100</pubDate>
            <guid isPermaLink="false">5526174</guid>        </item>
        <item>
            <title>Antivirus and immune enhancement activities of sulfated polysaccharide from Angelica sinensis.</title>
            <link>http://www.medworm.com/index.php?rid=5526146&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155400%26dopt%3DAbstract</link>
            <description>This study is to synthesize sulfated Angelica polysaccharides (APSs) and investigate the activity of one of the sulfated derivatives APS-1 on murine leukemia virus in vivo. Six sulfated derivatives with degree of sulfation ranging from 0.68 to 1.91 were obtained. And the virus replication was inhibited by APS-1 at the dose of 10 and 30mg/kg (26% and 30% inhibition respectively). Furthermore, both the percentage of CD4(+) cells and CD4(+)/CD8(+) ratio in peripheral blood cells were significantly enhanced by APS-1 at 3-30mg/kg. In addition, the reduced thymus/body weight index by murine leukemia virus infection was increased by ASP-1 in a dose dependent manner. These results suggest that APS-1 could not only inhibit virus replication, but also improve the immune function. APS-1 may be a pote...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526146</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526146</guid>        </item>
        <item>
            <title>Concentration selective hydration and phase states of hydroxyethyl cellulose (HEC) in aqueous solutions.</title>
            <link>http://www.medworm.com/index.php?rid=5526139&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155401%26dopt%3DAbstract</link>
            <description>Authors: Arfin N, Bohidar HB
    Abstract
    Solution behaviour of hydroxyethyl cellulose (HEC) is reported in the polymer concentration range spanning over two decades (c=0.002-5% (w/v)). The results conclude the following: (i) dilute solution regime prevailed for c&amp;lt;0.2% (w/v), flexible HEC fibres of typical length ≈1μm and persistence length ≈10nm were found here, (ii) for 0.2&amp;lt;c&amp;lt;1% (w/v), a semidilute phase comprising soluble aggregates of hydrated HEC fibrils were observed with the material exhibiting viscoelastic behaviour and (iii) when 1&amp;lt;c&amp;lt;5% (w/v) the solution behaved with melt-like attributes with substantial embedded heterogeneity; viscous to elastic transition was observed in this region. Raman spectral, and DSC data indicated distinctive hydration of HEC fib...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526139</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526139</guid>        </item>
        <item>
            <title>Laccase-mediated system pretreatment to enhance the effect of hydrogen peroxide bleaching of cotton fabric.</title>
            <link>http://www.medworm.com/index.php?rid=5526134&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155402%26dopt%3DAbstract</link>
            <description>This study evaluates the bleaching efficiency of the hydrogen peroxide bleaching process combined with laccase-mediated system pretreatment (LMS-HPBP) in the treatment of scoured cotton fabric. By changing the factors of laccase-mediated system pretreatment and the hydrogen peroxide bleaching process and examining the subsequent whiteness value and retained tensile strength of the samples, we find three LMS-HPBP processes that are more environment friendly than the conventional hydrogen peroxide bleaching process (CHPBP): (i) bleaching with lower dosage of hydrogen peroxide; (ii) bleaching at reduced temperature; (iii) bleaching for shortened duration. Whiteness, retained tensile strength and K/S values of cotton fabric samples treated by i-iii processes were similar to or higher than thos...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526134</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526134</guid>        </item>
        <item>
            <title>Adsorption of Hg(2+), Cu(2+) and Zn(2+) ions from aqueous solution using formaldehyde cross-linked modified chitosan.</title>
            <link>http://www.medworm.com/index.php?rid=5526133&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155403%26dopt%3DAbstract</link>
            <description>Authors: Monier M
    Abstract
    A chitosan-thioglyceraldehyde Schiff's base cross-linked magnetic resin (CSTG) was prepared and characterized using various instrumental methods. Then, the prepared resin was used for comparative studies on the removal of toxic metal ions like: Hg(2+), Cu(2+) and Zn(2+) from aqueous solutions. The effects of the initial pH value of the solution, contact time, the initial metal ion concentration and temperature on the adsorption capacity of the composite were investigated. The kinetics data were analyzed by pseudo-first order and pseudo-second order equations. The adsorption kinetics was well described by the pseudo-second order equation, and the adsorption isotherms were better fitted by the Langmuir equation. The maximum theoretical adsorption capacities...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526133</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526133</guid>        </item>
        <item>
            <title>Peptide screening to knockdown Bcl-2's anti-apoptotic activity: Implications in cancer treatment.</title>
            <link>http://www.medworm.com/index.php?rid=5526149&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155216%26dopt%3DAbstract</link>
            <description>This study suggests a new molecule that inhibits Bcl-2 associated cancer/tumor regression.
    PMID: 22155216 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526149</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526149</guid>        </item>
        <item>
            <title>An amperometric biosensor based on laccase immobilized onto MnO(2)NPs/cMWCNT/PANI modified Au electrode.</title>
            <link>http://www.medworm.com/index.php?rid=5526154&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22142791%26dopt%3DAbstract</link>
            <description>Authors: Rawal R, Chawla S, Malik P, Pundir CS
    Abstract
    A method is described for construction of an amperometric biosensor for detection of phenolic compounds based on covalent immobilization of laccase (Lac) onto manganese dioxide nanoparticles (MnO(2)NPs) decorated carboxylated multiwalled carbon nanotubes (cMWCNTs)/PANI composite electrodeposited onto a gold (Au) electrode through N-ethyl-N'-(3-dimethylaminopropyl) carbodiimide (EDC) and N-hydroxy succinimide (NHS) chemistry. The modified electrode was characterized by scanning electron microscopy (SEM), cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). The biosensor showed optimum response at pH 5.5 (0.1M sodium acetate buffer) and 35°C, when operated at 0.3V vs. Ag/AgCl. Linear range, response time, d...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526154</comments>
            <pubDate>Tue, 29 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526154</guid>        </item>
        <item>
            <title>Characterization of binding mode of imatinib to human α(1)-acid glycoprotein.</title>
            <link>http://www.medworm.com/index.php?rid=5526152&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22142793%26dopt%3DAbstract</link>
            <description>Authors: Fitos I, Simon A, Zsila F, Mády G, Bencsura A, Varga Z, Orfi L, Kéri G, Visy J
    Abstract
    Imatinib (IMT) is a selective tyrosine kinase inhibitor, used in the treatment of chronic myeloid leukemia and gastrointestinal stromal tumors. Its strong plasma protein binding was found to belong to the F1*S genetic variant of α(1)-acid glycoprotein (AGP). In this work, comparative AGP binding studies were performed with IMT fragment molecules to reveal which parts of the molecule are important in the high-affinity interaction provoking specific spectral changes. Molecular modeling calculations indicated that IMT docked into the X-ray structure of AGP/F1 adopts a bent, compact conformation. This binding mode is similar to those found in its complexes with some low-affinity kinases ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526152</comments>
            <pubDate>Tue, 29 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526152</guid>        </item>
        <item>
            <title>Immobilization of tyrosinase on chitosan-clay composite beads.</title>
            <link>http://www.medworm.com/index.php?rid=5526151&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155214%26dopt%3DAbstract</link>
            <description>Authors: Dinçer A, Becerik S, Aydemir T
    Abstract
    Tyrosinase was immobilized on glutaraldehyde crosslinked chitosan-clay composite beads and used for phenol removal. Immobilization yield, loading efficiency and activity of tyrosinase immobilized beads were found as 67%, 25% and 1400U/g beads respectively. Optimum pH of the free and immobilized enzyme was found as pH 7.0. Optimum temperature of the free and immobilized enzyme was determined as 25-30°C and 25°C respectively. The kinetic parameters of free and immobilized tyrosinase were calculated using l-catechol as a substrate and K(m) value for free and immobilized tyrosinase were found as 0.93mM and 1.7mM respectively. After seven times of repeated tests, each over 150min, the efficiency of phenol removal using same immobilized...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526151</comments>
            <pubDate>Tue, 29 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526151</guid>        </item>
        <item>
            <title>Carboxymethyl tamarind kernel polysaccharide nanoparticles for ophthalmic drug delivery.</title>
            <link>http://www.medworm.com/index.php?rid=5526155&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138451%26dopt%3DAbstract</link>
            <description>Authors: Kaur H, Ahuja M, Kumar S, Dilbaghi N
    Abstract
    Tropicamide-loaded carboxymethyl tamarind kernel polysaccharide (CMTKP) nanoparticles were prepared and evaluated for ocular delivery. Preparation of ionotropically gelled CMTKP nanoparticles was optimized employing three-levels, two-factor central composite design. Concentration of polymer and crosslinker had significant synergistic effect on particle size and % encapsulation efficiency. The optimal calculated parameters were concentrations of CMTKP 0.10% (w/v) and calcium chloride 0.11% (w/v). The optimized tropicamide-loaded CMTKP formulation showed ex vivo corneal permeation of tropicamide across isolated goat cornea comparable to its aqueous solution. Further, the mucoadhesive and non-irritant nature of CMTKP nanoparticles...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526155</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526155</guid>        </item>
        <item>
            <title>Synthesis, characterization and applications of graft copolymer (κ-carrageenan-g-vinylsulfonic acid).</title>
            <link>http://www.medworm.com/index.php?rid=5526153&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22142792%26dopt%3DAbstract</link>
            <description>Authors: Yadav M, Sand A, Mishra MM, Tripathy J, Pandey VS, Behari K
    Abstract
    The synthesis of graft copolymer (κ-carrageenan-g-vinylsulfonic acid) is carried out in nitrogen atmosphere using potassium peroxymonosulfate (PMS) and malonic acid (MA) as redox system. The effect of reaction variables including the concentration of vinylsulfonic acid 1.3×10(-2) to 6.7×10(-2)moldm(-3), PMS 4×10(-3) to 20×10(-3)moldm(-3), MA 1.6×10(-3) to 4.8×10(-3)moldm(-3), sulfuric acid 1×10(-3) to 8×10(-3)moldm(-3), κ-carrageenan 0.4-1.8gdm(-3) as well as time duration 60-180min and temperature 25-45°C has been studied. The water swelling capacity of graft copolymer is investigated. Flocculation property for both coking and non-coking coals is studied for the treatment of coal mine waste wa...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526153</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526153</guid>        </item>
        <item>
            <title>Practical synthesis and characterization of mannose-modified chitosan.</title>
            <link>http://www.medworm.com/index.php?rid=5526150&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155215%26dopt%3DAbstract</link>
            <description>Authors: Yao W, Jiao Y, Luo J, Du M, Zong L
    Abstract
    A new and practical laboratory approach to synthesize mannose modified chitosan (Man-chitosan) was developed via reductive amination reaction. Chitosan and mannose were used as raw materials. The reaction condition was mild and controllable. The overall yield was 47-52%. Each reaction products and Man-chitosan were characterized by (1)H NMR, ESI-MS, FT-IR and TGA spectrum. FT-IR and (1)H NMR results showed that mannose conjugated to chitosan via an alkane chain bridge (CH(2)CH(2)). The degree of substitution was calculated by element analysis. TGA results indicated that mannose grafted to chitosan slightly decreased the thermal stability of chitosan in some extent. MTT assay indicated that Man-chitosan was low cytotoxicity agains...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526150</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526150</guid>        </item>
        <item>
            <title>Extraction, purification and antibacterial activities of a polysaccharide from spent mushroom substrate.</title>
            <link>http://www.medworm.com/index.php?rid=5526168&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138450%26dopt%3DAbstract</link>
            <description>Authors: Zhu H, Sheng K, Yan E, Qiao J, Lv F
    Abstract
    To contribute towards effective exploitation and utilization of spent mushroom substrate (SMS), a water-soluble polysaccharide named PL was isolated and purified from SMS. The total sugar content and monosaccharide composition were analyzed by phenol-sulfuric acid method and capillary electrophoresis, and infrared spectroscopy was also performed for structure characterization. The results showed that the total sugar content of crude polysaccharide from SMS was about 25.8%, the polysaccharide contained two fractions (PL1 and PL2), which was mainly composed of glucose, rhamnose and mannose with a molar ratio of 1:3.13:1.16. The attributions of the main absorptions of both PL1 and PL2 were characteristic of glycosidic structures, a...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526168</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526168</guid>        </item>
        <item>
            <title>Probing the role of asparagine mutation in thermostability of Bacillus KR-8104 α-amylase.</title>
            <link>http://www.medworm.com/index.php?rid=5526173&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22126991%26dopt%3DAbstract</link>
            <description>Authors: Rahimzadeh M, Khajeh K, Mirshahi M, Khayatian M, Schwarzenbacher R
    Abstract
    Asparagine deamidation is one of the important determinants of protein thermostability. Here, structure based mutagenesis has been done in order to probe the role of Asn residues in thermostability of a Ca independent Bacillus sp. KR-8104 α-amylase (BKA). Residues involved in potential deamidation processes have been selected and replaced using a site directed mutagenesis. Fourteen different variants were tested for thermostability by measuring residual activities after incubation at high temperature. In comparison to the wild-type enzyme, four mutated variants are able to increase the half life of the protein at high temperatures. The highest stabilization resulted from the substitution of aspara...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526173</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526173</guid>        </item>
        <item>
            <title>An immunostimulatory polysaccharide (SCP-IIa) from the fruit of Schisandra chinensis (Turcz.) Baill.</title>
            <link>http://www.medworm.com/index.php?rid=5526171&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22133665%26dopt%3DAbstract</link>
            <description>Authors: Chen Y, Tang J, Wang X, Sun F, Liang S
    Abstract
    A water-soluble polysaccharide named SCP-IIa was isolated from the water extract of the fruit of Schisandra chinensis (Turcz.) Baill by means of ethanol precipitation, deproteination, anion-exchange and gel-permeation chromatography. The molecular weight of SCP-IIa was ascertained via HPLC, and immuno-modulating effect was evaluated using the immunosuppressed model induced by cyclophosphamide. SCP-IIa was a homogeneous form of polysaccharide, with an average molecular weight of approximately 7700Da. The detected parameters showed that SCP-IIa increased the thymus and spleen indices, as well as the pinocytic activity of the peritoneal macrophages in immunosuppressed mice. The splenocyte proliferation assay showed that SCP-IIa,...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526171</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526171</guid>        </item>
        <item>
            <title>DNA conformational equilibrium in the presence of Zn(2+) ions in neutral and alkaline solutions.</title>
            <link>http://www.medworm.com/index.php?rid=5526176&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22119960%26dopt%3DAbstract</link>
            <description>Authors: Sorokin VA, Valeev VA, Usenko EL, Andrushchenko VV
    Abstract
    Effect of Zn(2+) ions on DNA transition from B-form to a metallized form (m-DNA) in Tris and tetraborate buffers at pH 8.5 has been studied by visible and differential UV-spectroscopy and by thermal denaturation. The results have been compared to those obtained at pH 6.5 in cacodylate buffer. It was found that in alkaline solutions Zn(2+) ions induced a hypochromicity of the DNA absorption in the whole spectral range monitored, which was attributed to DNA transition from B- to the m-form. Complete metallization occurred only upon heating the DNA solutions containing more than ∼2×10(-4)M of Zn(2+) ions. Phase diagrams of the DNA-zinc complexes at pH 6.5 and 8.5 have been obtained for the first time. The m-DNA fo...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526176</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526176</guid>        </item>
        <item>
            <title>Composition and antioxidant activity of the polysaccharides from cultivated Saussurea involucrata.</title>
            <link>http://www.medworm.com/index.php?rid=5526175&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120502%26dopt%3DAbstract</link>
            <description>Authors: Yao L, Zhao Q, Xiao J, Sun J, Yuan X, Zhao B, Su H, Niu S
    Abstract
    Polysaccharides from cultivated Saussurea involucrata (CSIP) were purified, two major fractions (CSIP1-2 and CSIP2-3) were investigated for their molecular weights, monosaccharide compositions and in vitro antioxidant activities. The results suggested that the molecular weights of CSIP1-2 and CSIP2-3 were approximately 163.5kDa and 88.6kDa, respectively. CSIP1-2 was composed of glucose, galactose, xylose, rhamnose, arabinose and galacturonic acid with a molar ratio of 1.651:0.39:0.062:8.331:1.759:40.426. CSIP2-3 was composed of glucose, galactose, xylose, rhamnose, arabinose and galacturonic acid with a molar ratio of 0.762:0.657:0.112:5.587:0.318:44.655. Different scavenging activities on superoxide radica...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526175</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526175</guid>        </item>
        <item>
            <title>Mechanistic insights into protein precipitation by alcohol.</title>
            <link>http://www.medworm.com/index.php?rid=5526179&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22115717%26dopt%3DAbstract</link>
            <description>Authors: Yoshikawa H, Hirano A, Arakawa T, Shiraki K
    Abstract
    Ethanol is used to precipitate proteins during various processes, including purification and crystallization. To elucidate the mechanism of protein precipitation by alcohol, we have investigated the solubility and structural changes of protein over a wide range of alcohol concentrations. Conformation of hen egg-white lysozyme was changed from native to α-helical rich structure in the presence of ethanol at concentrations above 60%. The solubility of lysozyme was reduced with increasing ethanol concentration, although gel formation at ethanol concentrations between 60% and 75% prevented accurate solubility measurements. SH-modified lysozyme showed largely unfolded structure in water and α-helical structure in the presen...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526179</comments>
            <pubDate>Fri, 18 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526179</guid>        </item>
        <item>
            <title>Facile production of chitin from crab shells using ionic liquid and citric acid.</title>
            <link>http://www.medworm.com/index.php?rid=5526182&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22108289%26dopt%3DAbstract</link>
            <description>Authors: Setoguchi T, Kato T, Yamamoto K, Kadokawa JI
    Abstract
    Facile production of chitin from crab shells was performed by direct extraction using an ionic liquid, 1-allyl-3-methylimidazolium bromide (AMIMBr), followed by demineralization using citric acid. First, dried crab shells were treated with AMIMBr at elevated temperatures to extract chitin. Supernatants separated by centrifugation were then subjected to a chelating treatment with an aqueous solution of citric acid to achieve demineralization. The precipitated extracts were filtered and dried. The isolated material was subjected to X-ray diffraction, IR, (1)H NMR, and energy-dispersive X-ray spectroscopy, and thermal gravimetric analysis; the results indicated the structure of chitin. On the basis of the IR spectra, the d...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526182</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526182</guid>        </item>
        <item>
            <title>WITHDRAWN: Preparation and characterization of silica gel/chitosan composite for the removal of Cu(II) and Pb(II).</title>
            <link>http://www.medworm.com/index.php?rid=5526185&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100868%26dopt%3DAbstract</link>
            <description>This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy.
    PMID: 22100868 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526185</comments>
            <pubDate>Wed, 09 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526185</guid>        </item>
        <item>
            <title>Antinociception of β-d-glucan from Pleurotus pulmonarius is possibly related to protein kinase C inhibition.</title>
            <link>http://www.medworm.com/index.php?rid=5526198&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22085751%26dopt%3DAbstract</link>
            <description>This study evaluated the involvement of transient receptor potential (TRP) channels and protein kinase C (PKC) on antinociceptive effect of a (1→3),(1→6)-linked β-d-glucan (GL) in mice. Intraperitoneal administration of GL potently inhibited nociceptive responses induced by intraplantar injections of capsaicin, cinnamaldehyde, menthol, acidified saline and phorbol myristate acetate (PMA). Moreover, Western blot analysis revealed that GL treatment also prevented PMA-induced PKCɛ activation. Collectively, present results demonstrate that GL could constitute an attractive molecule of interest for the development of new analgesic drugs.
    PMID: 22085751 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5526198</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5526198</guid>        </item>
        <item>
            <title>Optimization on preparation condition of epimedium polysaccharide liposome and evaluation of its adjuvant activity.</title>
            <link>http://www.medworm.com/index.php?rid=5412313&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22074742%26dopt%3DAbstract</link>
            <description>Authors: Gao H, Fan Y, Wang D, Hu Y, Liu J, Zhao X, Guo L, Zhao X, Yuan J, Zhang F
    Abstract
    The aim of this strategy was to investigate whether the adjuvant activity of epimedium polysaccharide (EPS) could be further enhanced after encapsulated with liposome. In preparation of EPS liposome (EPSL) test, an orthogonal L(9) (3(4)) test design was used to optimize the preparation condition of EPSL. In adjuvant activity test, 350 14-day-old chickens were randomly assigned to 7 groups and vaccinated with Newcastle disease (ND) vaccine. Simultaneously, the chickens in experimental groups were injected with EPSL at three doses, EPS and blank liposome, respectively. The activity of lymphocytes proliferation, titer of serum antibody and concentrations of cytokines were determined. Results sh...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412313</comments>
            <pubDate>Sat, 29 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412313</guid>        </item>
        <item>
            <title>Immobilization of lipase on cotton cloth using the layer-by-layer self-assembly technique.</title>
            <link>http://www.medworm.com/index.php?rid=5412315&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062119%26dopt%3DAbstract</link>
            <description>Authors: Karimpil JJ, Melo JS, D'Souza SF
    Abstract
    Lipase from Thermomyces lanuginosus was assembled into multiple layers on polyethylenimine treated cotton flannel cloth, utilising the enzymes property of forming bimolecular aggregates via layer-by-layer (LBL) immobilization technique. An increase in lipase activity with increasing enzyme layers confirmed lipase aggregation. A study to compare the activity of enzyme bound by classical LBL technique, containing alternate layers of polyethylenimine and lipase and the modified approach indicated above, showed that more enzyme was bound to cloth in the modified approach. A total of 13U/cm(2) of enzyme were bound to cloth till the fifth layer whereas only 10.2U/cm(2) were bound till the fifth bilayer in the classical approach. The succ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412315</comments>
            <pubDate>Fri, 28 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412315</guid>        </item>
        <item>
            <title>Interpenetrating polymer network (IPN) hydrogel microspheres for oral controlled release application.</title>
            <link>http://www.medworm.com/index.php?rid=5412314&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062120%26dopt%3DAbstract</link>
            <description>Authors: Banerjee S, Siddiqui L, Bhattacharya SS, Kaity S, Ghosh A, Chattopadhyay P, Pandey A, Singh L
    Abstract
    Interpenetrating polymer network (IPN) hydrogel microspheres of sodium carboxymethyl cellulose (NaCMC) and poly(vinyl alcohol) (PVA) were prepared by water-in-oil (w/o) emulsion crosslinking method for oral controlled release delivery of a non-steroidal anti-inflammatory drug, diclofenac sodium. The microspheres were prepared with various ratios of NaCMC to PVA, % drug loading and extent of crosslinking density at a fixed polymer weight. The prepared microspheres with loose and rigid surfaces were evidenced by scanning electron microscope (SEM). Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) analysis confirmed the IPN formation differential sca...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412314</comments>
            <pubDate>Fri, 28 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412314</guid>        </item>
        <item>
            <title>Analysis of the interactions between Eudragit(®) L100 and porcine pancreatic trypsin by calorimetric techniques.</title>
            <link>http://www.medworm.com/index.php?rid=5412318&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057084%26dopt%3DAbstract</link>
            <description>Authors: Braia M, Tubio G, Nerli B, Loh W, Romanini D
    Abstract
    Flexible-chain polymers with charge (polyelectrolytes) can interact with globular proteins with a net charge opposite to the charge of the polymers forming insoluble complexes polymer-protein. In this work, the interaction between the basic protein trypsin and the anionic polyelectrolyte Eudragit(®) L100 was studied by using isothermal calorimetric titrations and differential scanning calorimetry. Turbidimetric assays allowed determining that protein-polymer complex was insoluble at pH below 5 and the trypsin and Eudragit(®) L100 concentrations required forming the insoluble complex. DSC measurements showed that the T(m) and denaturalization heat of trypsin increased in the polymer presence and the complex unfolded ac...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412318</comments>
            <pubDate>Tue, 25 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412318</guid>        </item>
        <item>
            <title>5α-Reductase inhibitors, antiviral and anti-tumor activities of some steroidal cyanopyridinone derivatives.</title>
            <link>http://www.medworm.com/index.php?rid=5412317&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057085%26dopt%3DAbstract</link>
            <description>Authors: Al-Mohizea AM, Al-Omar MA, Abdalla MM, Amr AG
    Abstract
    We herein report the 5α-reductase inhibitors, antiviral and anti-tumor activities of some synthesized heterocyclic cyanopyridone and cyanothiopyridone derivatives fused with steroidal structure. Initially the acute toxicity of the compounds was assayed via the determination of their LD(50). All the compounds, except 3b, were interestingly less toxic than the reference drug (Prednisolone(®)). Seventeen heterocyclic derivatives containing a cyanopyridone or cyanothiopyridone rings fused to a steroidal moiety were synthesized and screened for their 5α-reductase inhibitors, antiviral and anti-tumor activities comparable to that of Anastrozole, Bicalutamide, Efavirenz, Capravirine, Ribavirin, Oseltamivir and Amantadine a...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412317</comments>
            <pubDate>Tue, 25 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412317</guid>        </item>
        <item>
            <title>Anti-amyloidogenic and fibril-destabilizing effects of two manganese-salen derivatives against hen egg-white lysozyme aggregation.</title>
            <link>http://www.medworm.com/index.php?rid=5412316&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22061184%26dopt%3DAbstract</link>
            <description>Authors: Bahramikia S, Yazdanparast R
    Abstract
    Amyloid depositions of proteins play crucial roles in a wide variety of degenerative disorders called amyloidosis. In the present study, we used hen egg white lysozyme (HEWL), as an in vitro model system, to induce fibrillation under high temperatures and acidic pH conditions, and investigated the inhibitory and disruptive effects of two salen-manganese complexes, namely EUK-8 and EUK-134, with aromatic structures, against fibrilization. Results of this study showed that EUK-8 and EUK-134in a dose-dependent manner inhibited the HEWL aggregation. Similar results were obtained when these compounds were added to pre-formed amyloid fibrils. Docking results also demonstrated that the aromatic rings of EUK-8 and EUK-134 interact with the hyd...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5412316</comments>
            <pubDate>Tue, 25 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5412316</guid>        </item>
        <item>
            <title>Glycolic acid-g-chitosan-gold nanoflower nanocomposite scaffolds for drug delivery and tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5376811&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22044748%26dopt%3DAbstract</link>
            <description>Authors: Kumari S, Singh RP
    Abstract
    This paper reports a simple novel method for the synthesis of flower like gold nanoparticle (three dimensional branched nanoparticle) with &amp;gt;30 tips, under controlled temperature condition. Formation of flower like Au nanoparticle was confirmed by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Next step of this paper reveals the potential use of novel hybrids of chitosan-g-glycolic acid and gold nanoflower (AuNF) in controlled drug delivery and tissue engineering applications. The drug loaded novel nanohybrid scaffold is prepared by freeze drying of grafted polymer solution. Grafting of glycolic acid to the chitosan and incorporation of drug were evaluated by Fourier transform infrared spectroscopy (FTIR). The n...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376811</comments>
            <pubDate>Sun, 23 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376811</guid>        </item>
        <item>
            <title>Effects of the polysaccharide from Pholiota nameko on human cytokine network in serum.</title>
            <link>http://www.medworm.com/index.php?rid=5376810&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22044749%26dopt%3DAbstract</link>
            <description>Authors: Li H, Liu X, Li Y, Hua Y, Zhi D, Pang G
    Abstract
    Some physico-chemical characterizations of Pholiota nameko polysaccharides (PNPS-1) were studied, including sulfate content, UV/visible and infrared spectra, also the variation of cytokine communication network in serum to clarify the pharmacological effects of PNPS-1 by determination of 39 cytokines in serum of healthy volunteers. The result proved that PNPS-1 possessed significant anti-inflammatory activity. Further, we use Microsoft Visio 2007 software to map out the cell-cell communication network diagram. The analysis to the diagram suggested that PNPS-1 could take effect on the innate and adaptive immunity and hematopoiesis of volunteers.
    PMID: 22044749 [PubMed - as supplied by publisher] (Source: International Jou...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376810</comments>
            <pubDate>Sun, 23 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376810</guid>        </item>
        <item>
            <title>Preparation of chondroitin sulfate nanocapsules for use as carries by the interfacial polymerization method.</title>
            <link>http://www.medworm.com/index.php?rid=5376813&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22033115%26dopt%3DAbstract</link>
            <description>Authors: Xi J, Zhou L, Fei Y
    Abstract
    In this paper, the method of interfacial polymerization in emulsion was employed to fabricate chondroitin sulfate-methacrylate (ChSMA) nanocapsules, in which poor water-soluble drug of indomethacin (IND) could be effectively encapsulated. The morphology and the size distribution of synthesized nanocapsules were characterized by field emission scanning electron microscopy (FESEM) and dynamic light scattering (DLS) techniques. The quantitative drug loading was investigated. The IND/ChSMA noodle-like self-assemblies were observed with the increase of IND feed concentration, and the interactions between IND and ChSMA were illuminated by FT-IR and XRD measurements. The in vitro drug release of IND-loaded nanocapsules and IND/ChSMA self-assemblies we...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376813</comments>
            <pubDate>Thu, 20 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376813</guid>        </item>
        <item>
            <title>Structure of Fab fragment of malaria transmission blocking antibody 2A8 against P. vivax P25 protein.</title>
            <link>http://www.medworm.com/index.php?rid=5376812&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22037467%26dopt%3DAbstract</link>
            <description>We report here the crystallization and X-ray structure of native Fab2A8 at 4.0Å resolution. The 2A8 antibody generated against Pvs25 prevents the formation of P. vivax oocysts in the mosquito, when assayed in membrane feeding experiment. Comparison of native Fab2A8 structure with antigen bound Fab2A8 structure indicates the significant conformational changes in CDR-H1 and CDR-H3 regions of V(H) domain and CDR-L3 region of V(L) domain of Fab2A8. Upon complex formation, the relative orientation between V(L) and V(H) domains of Fab2A8 is conserved, while significant differences are observed in elbow angles of heavy and light chains. The combing site residues of complexed Fab2A8 exhibited the reduced temperature factor compared to native Fab2A8, suggesting a loss of conformational entropy up...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376812</comments>
            <pubDate>Thu, 20 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376812</guid>        </item>
        <item>
            <title>Composition and characterization of an acidic polysaccharide from out-of-date tea leaves.</title>
            <link>http://www.medworm.com/index.php?rid=5376824&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22019982%26dopt%3DAbstract</link>
            <description>Authors: Xiao J, Huo J, Jiang H, Yamamoto K
    Abstract
    An acidic polysaccharide conjugate from the tea leaves (Camellia sinensis) beyond the useful date was isolated and characterized. The crude polysaccharides (TPS) were extracted with hot water and separated on a DEAE sepharose FF gel filtration column to obtain ATPS2. The chemical structure of ATPS2 was investigated by GC, IC, HPGPC, IR, UV, Periodate oxidation-Smith degradation, (1)H NMR, and (13)C NMR methods and its conformation was observed with Congo red test. The crude TPS mainly consisted of 5 peaks with molecular weights of 7.67×10(5), 2.03×10(5), 2.83×10(4), 3470.2, and 1205.52Da, respectively. The molecular weight of ATPS2 was determined as 7.4×10(5)Da by HPGPC. IC chromatogram of ATPS2 showed that ATPS2 consisted of...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376824</comments>
            <pubDate>Mon, 17 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376824</guid>        </item>
        <item>
            <title>Evaluation of chitoligosaccharides effect upon probiotic bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=5376814&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22024313%26dopt%3DAbstract</link>
            <description>Authors: Fernandes JC, Eaton P, Franco I, Ramos OS, Sousa S, Nascimento H, Gomes A, Santos-Silva A, Xavier Malcata F, Pintado ME
    Abstract
    The main objective of the present study was to evaluate the antibacterial effect - through the determination of minimum inhibitory (and lethal) concentrations, as well as the possible prebiotic potential of chitooligosaccharides (COS) - through the determination of growth curves, on Bifidobacterium animalis Bb12, Bifidobacterium animalis Bo and Lactobacillus acidophilus Ki. Atomic force microscopy was further used to obtain high resolution images of COS effects upon the cell morphology. Our results demonstrate that COS do not stimulate the growth of those strains, neither the strains are capable of using COS as a primary source of carbon. Analysi...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376814</comments>
            <pubDate>Mon, 17 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376814</guid>        </item>
        <item>
            <title>Galactomannan thin films as supports for the immobilization of Concanavalin A and/or dengue viruses.</title>
            <link>http://www.medworm.com/index.php?rid=5376823&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020153%26dopt%3DAbstract</link>
            <description>Authors: Valenga F, Petri DF, Lucyszyn N, Jó TA, Sierakowski MR
    Abstract
    The immobilization of the glucose/mannose-binding lectin from Concanavalia ensiformis seeds (ConA) onto a monolayer made of a galactomannan extracted from Leucaena leucocephala seeds (GML), which was adsorbed onto - amino-terminated surfaces, was investigated by means of ellipsometry and atomic force microscopy. The mean thickness of GML monolayer, which polysaccharide consists of linear 1→4-linked β-d-mannopyranosil units partially substituted at C-6 by α-d-galactopyranosyl units, amounted to (1.5±0.2)nm. ConA molecules adsorbed onto GML surfaces forming (2.0±0.5)nm thick layers. However, in the presence of mannose the adsorption failed, indicating that ConA binding sites were blocked by mannose and we...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376823</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376823</guid>        </item>
        <item>
            <title>A possible structure of retrograded maize starch speculated by UV and IR spectra of it and its components.</title>
            <link>http://www.medworm.com/index.php?rid=5376822&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020154%26dopt%3DAbstract</link>
            <description>Authors: Lian X, Zhang K, Luo Q, Wang C, Liu X
    Abstract
    &quot;Retrogradation&quot; has been used to describe the changes that occur in starch after gelatinization, from an initially amorphous state to a more ordered or crystalline state, which has a significant impact on starch application in food, textiles and materials fields. But mechanism of starch retrogradation is still unclear until now and there is no breakthrough in this area. Here we are speculating a possible structure of retrograded maize starch by UV (binding with iodine) and IR spectra of it and its compositions. We speculate that nucleation of retrograded starch origins from combination of reducing end of amylopectin and non-reducing end of amylose, and retrogradation terminates at combining of non-reducing end of amylopectin ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376822</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376822</guid>        </item>
        <item>
            <title>Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262.</title>
            <link>http://www.medworm.com/index.php?rid=5376821&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020155%26dopt%3DAbstract</link>
            <description>Authors: Kim S, Bae SY, Kim SJ, Ngo TD, Kim KK, Kim TD
    Abstract
    A novel oligomeric hydrolase (LI22) from Listeria innocua CLIP 11262 was identified, characterized, and immobilized for industrial application. Sequence analysis of LI22 revealed a putative catalytic triad (Ser(10)-Asp(176)-His(179)), and a conserved sequence motif Ser(S)(10)-Gly(G)(77)-Asn(N)(79)-His(H)(179) with moderate identities (&amp;lt;30%) with other members of the SGNH-hydrolase superfamily. LI22 was able to hydrolyze p-nitrophenyl acetate, α- and β-naphthyl acetate, while the S10A mutant completely lost its activity. Structural properties of LI22 were investigated using gel filtration, circular dichroism (CD), fluorescence, molecular modeling, and gel filtration. We have shown that upon incubation in 30% TFE or...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376821</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376821</guid>        </item>
        <item>
            <title>Halophilic characterization of starch-binding domain from Kocuria varians α-amylase.</title>
            <link>http://www.medworm.com/index.php?rid=5376820&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020156%26dopt%3DAbstract</link>
            <description>Authors: Yamaguchi R, Inoue Y, Tokunaga H, Ishibashi M, Arakawa T, Sumitani JI, Kawaguchi T, Tokunaga M
    Abstract
    The tandem starch-binding domains (KvSBD) located at carboxy-terminal region of halophilic α-amylase from moderate halophile, Kocuria varians, were expressed in E. coli with amino-terminal hexa-His-tag and purified to homogeneity. The recombinant KvSBD showed binding activity to raw starch granules at low to high salt concentrations. The binding activity of KvSBD to starch was fully reversible after heat-treatment at 85°C. Circular dichroism and thermal scanning experiments indicated that KvSBD showed fully reversible refolding upon cooling after complete melting at 70°C in the presence of 0.2-2.0M NaCl. The refolding rate was enhanced with higher salt concentration.
...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376820</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376820</guid>        </item>
        <item>
            <title>Liposome and epimedium polysaccharide-propolis flavone can synergistically enhance immune effect of vaccine.</title>
            <link>http://www.medworm.com/index.php?rid=5376819&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020157%26dopt%3DAbstract</link>
            <description>Authors: Fan Y, Wang D, Hu Y, Liu J, Han G, Zhao X, Yuan J, Liu C, Liu X, Ni X
    Abstract
    Three preparations of epimedium polysaccharide-propolis flavone immunopotentiator (EPI), EPI liposome, EPI suspension and EPI watery solution were prepared. In immune response test, their adjuvanticities were compared in 14-day-old chickens vaccinated with Newcastle disease (ND) vaccine. In immune protection test, the effects of the three preparations on Newcastle disease virus (NDV) infection were compared in chickens vaccinated with ND vaccine then challenged with NDV. The results displayed that EPI liposome could enhance the antibody titer, T lymphocyte proliferation and the concentrations of interferon-γ and interleukin-6, when compared with the other two preparations. In EPI liposome group...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376819</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376819</guid>        </item>
        <item>
            <title>Physicochemical properties and in vitro digestibility of flour and starch from pea (Pisum sativum L.) cultivars.</title>
            <link>http://www.medworm.com/index.php?rid=5376818&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020158%26dopt%3DAbstract</link>
            <description>Authors: Chung HJ, Liu Q
    Abstract
    Flours and isolated starches from three different cultivars (1544-8, 1658-11 and 1760-8) of pea grown under identical environmental conditions were evaluated for their physicochemical properties and in vitro digestibility. The protein content, total starch content and apparent amylose content of pea flour ranged from 24.4 to 26.3%, 48.8 to 50.2%, and 13.9 to 16.7%, respectively. In pea starches, the 1760-8 showed higher apparent amylose content and total starch content than the other cultivars. Pea starch granules were irregularly shaped, ranging from oval to round with a smooth surface. All pea starches showed C-type X-ray diffraction pattern with relative crystallinity ranging between 23.7 and 24.7%. Pea starch had only a single endothermic trans...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376818</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376818</guid>        </item>
        <item>
            <title>Preparation and characterization of chitosan-polyvinyl alcohol blend hydrogels for the controlled release of nano-insulin.</title>
            <link>http://www.medworm.com/index.php?rid=5376817&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020189%26dopt%3DAbstract</link>
            <description>Authors: Zu Y, Zhang Y, Zhao X, Shan C, Zu S, Wang K, Li Y, Ge Y
    Abstract
    Chitosan (CS)-polyvinyl alcohol (PVA) blend hydrogels were prepared using glutaraldehyde as the cross-linking agent. The obtained hydrogels, which have the advantages of both PVA and CS, can be used as a material for the transdermal drug delivery (TDD) of insulin. The nano-insulin-loaded hydrogels were prepared under the following conditions: 1.2g of polyethylene glycol, 1.5g of CS, 1.2g of PVA, 1.2mL of 1% glutaraldehyde solution, 16mL of water, and 40mg of nano-insulin with 12min of mixing time and 3min of cross-linking time. The nano-insulin-loaded hydrogels were characterized using scanning electron microscopy, energy dispersive spectrometry, Fourier-transform infrared spectroscopy, differential scanning ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376817</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376817</guid>        </item>
        <item>
            <title>Construction of amperometric uric acid biosensor based on uricase immobilized on PBNPs/cMWCNT/PANI/Au composite.</title>
            <link>http://www.medworm.com/index.php?rid=5376816&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020190%26dopt%3DAbstract</link>
            <description>Authors: Rawal R, Chawla S, Chauhan N, Dahiya T, Pundir CS
    Abstract
    A chitosan-glutaraldehyde crosslinked uricase was immobilized onto Prussian blue nanoparticles (PBNPs) absorbed onto carboxylated multiwalled carbon nanotube (c-MWCNT) and polyaniline (PANI) layer, electrochemically deposited on the surface of Au electrode. The nanohybrid-uricase electrode was characterized by scanning electron microscopic (SEM), Fourier transform infrared spectroscopy (FTIR) and cyclic voltammetry. An amperometric uric acid biosensor was fabricated using uricase/c-MWCNT/PBNPs/Au electrode as working electrode, Ag/AgCl as standard and Pt wire as auxiliary electrode connected through a potentiostat. The biosensor showed optimum response within 4s at pH 7.5 and 40°C, when operated at 0.4V vs. Ag/AgC...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376816</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376816</guid>        </item>
        <item>
            <title>Development of cloxacillin loaded multiple-unit alginate-based floating system by emulsion-gelation method.</title>
            <link>http://www.medworm.com/index.php?rid=5376815&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020191%26dopt%3DAbstract</link>
            <description>Authors: Malakar J, Nayak AK, Pal D
    Abstract
    This work investigates the development, optimization and in vitro evaluation of liquid paraffin-entrapped multiple-unit alginate-based floating system containing cloxacillin by emulsion-gelation method for gastro retentive delivery. The effect of process variables like drug to polymer ratio by weight, and liquid paraffin to water ratio by volume on various physicochemical properties in case of liquid paraffin-entrapped calcium alginate beads containing cloxacillin applicable to drug entrapment efficiency, density and drug release was optimized using 3(2) factorial design and analyzed using response surface methodology. The observed (actual values) responses were coincided well with the predicted values, given by the optimization techniqu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376815</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376815</guid>        </item>
        <item>
            <title>Comparative characterization of aqueous dispersions and cast films of different chitin nanowhiskers/nanofibers.</title>
            <link>http://www.medworm.com/index.php?rid=5376827&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22001722%26dopt%3DAbstract</link>
            <description>Authors: Fan Y, Fukuzumi H, Saito T, Isogai A
    Abstract
    Water dispersions of TEMPO-oxidized α-chitin nanowhisker (TOChN), partially deacetylated α-chitin nanowhisker/nanofiber mixture (DEChN), HCl-hydrolyzed chitin nanowhisker (HHChN) and squid-pen β-chitin nanofiber (SQChN) were prepared, and the properties of nano-dispersions and their cast films were characterized between the four chitin nano-samples. Because SQChN has the highest aspect ratio, its 0.1% dispersion had the highest shear stress and viscosity at the same shear rate in the four chitin nano-samples, and showed gel-like behavior in the whole shear rate range from 10(-3) to 10(3) s(-1). AFM images of the self-standing films showed that film surfaces consisted of characteristic chitin nano-elements with different morp...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376827</comments>
            <pubDate>Thu, 06 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376827</guid>        </item>
        <item>
            <title>Characterization and in vitro immunomodulatory screening of fructo-oligosaccharides of Asparagus racemosus Willd.</title>
            <link>http://www.medworm.com/index.php?rid=5376826&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22001723%26dopt%3DAbstract</link>
            <description>Authors: Thakur M, Connellan P, Deseo MA, Morris C, Praznik W, Loeppert R, Dixit VK
    Abstract
    Asparagus racemosus Linn. (Fam. Liliaceae) is an ethno-pharmacologically acclaimed Ayurvedic medicinal plant. In the present study, aqueous extract of A. racemosus (ARC) was fractionated and screened for the polysaccharide fraction (ARP). The characterization was done by enzymatic, Size Exclusion, gas chromatography with flame ionization detector (GC-FID), high pressure anion exchange chromatography (HPAEC) and thin layer chromatographic analyses. Phyto-chemical evaluation confirmed the presence of 26.7% of 2→1 linked fructo-oligosaccharides (FOS). They have a degree of polymerization (DP) of nearly 9-10. Cytotoxicity evaluation on P388 cell lines was consistent with low cytotoxicity of t...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376826</comments>
            <pubDate>Thu, 06 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376826</guid>        </item>
        <item>
            <title>Study on the microstructure of African wild silk cocoon shells and fibers.</title>
            <link>http://www.medworm.com/index.php?rid=5376829&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21986544%26dopt%3DAbstract</link>
            <description>Authors: Teshome A, Vollrath F, Raina SK, Kabaru JM, Onyari J
    Abstract
    Silk fibers and cocoon shells from four African wild silkmoths Gonometa postica, Anaphe panda, Argema mimosae and Epiphora bauhiniae-were studied to gain insight into the structure-property-function relations and potential commercial application. The surface and cross-section of cocoon shells and fibers revealed the presence of prominent structural variations. Cocoon shells were multilayered and porous structures constructed from highly cross-linked fibers that are densely packed within the sericin/gum. Fibers had fibrillar sub-structures running along the fiber axis and with greater number and size of voids. The ecological significance and implication of these structures for further application are discussed.
 ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376829</comments>
            <pubDate>Wed, 05 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376829</guid>        </item>
        <item>
            <title>Synthesis and anticoagulant activity of the quaternary ammonium chitosan sulfates.</title>
            <link>http://www.medworm.com/index.php?rid=5376828&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21996571%26dopt%3DAbstract</link>
            <description>Authors: Fan L, Wu P, Zhang J, Gao S, Wang L, Li M, Sha M, Xie W, Nie M
    Abstract
    Quaternary ammonium chitosan sulfates with diverse degrees of substitution (DS) ascribed to sulfate groups between 0.52 and 1.55 were synthesized by reacting quaternary ammonium chitosan with an uncommon sulfating agent (N(SO(3)Na)(3)) that was prepared from sodium bisulfite (NaHSO(3)) through reaction with sodium nitrite (NaNO(2)) in the aqueous system homogeneous. The structures of the derivatives were characterized by FTIR, (1)H NMR and (13)C NMR. The factors affecting DS of quaternary ammonium chitosan sulfates which included the molar ratio of NaNO(2) to quaternary ammonium chitosan, sulfated temperature, sulfated time and pH of sulfated reaction solution were investigated in detail. Its anticoagu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376828</comments>
            <pubDate>Wed, 05 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376828</guid>        </item>
        <item>
            <title>Purification and characterization of YxeI, a penicillin acylase from Bacillus subtilis.</title>
            <link>http://www.medworm.com/index.php?rid=5376838&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21978958%26dopt%3DAbstract</link>
            <description>Authors: Rathinaswamy P, Gaikwad SM, Suresh CG, Prabhune AA, Brannigan JA, Dodson GG, Pundle AV
    Abstract
    The paper reports the purification and characterization of the first penicillin acylase from Bacillus subtilis. YxeI, the protein annotated as hypothetical, coded by the gene yxeI in the open reading frame between iol and hut operons in B. subtilis was cloned and expressed in Eshcherichia coli, purified and characterized. The purified protein showed measurable penicillin acylase activity with penicillin V. The enzyme was a homotetramer of 148kDa. The apparent K(m) of the enzyme for penicillin V and the synthetic substrate 2-nitro-5-(phenoxyacetamido)-benzoic acid was 40mM and 0.63mM, respectively, and the association constants were 8.93×10(2)M(-1) and 2.51×10(5)M(-1), respecti...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376838</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376838</guid>        </item>
        <item>
            <title>Preparation and characterization of nano-hydroxyapatite/chitosan cross-linking composite membrane intended for tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5376835&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21983025%26dopt%3DAbstract</link>
            <description>Authors: Li X, Nan K, Shi S, Chen H
    Abstract
    In this paper, a series of nano-hydroxyapatite(n-HA)/chitosan cross-linking composite membranes (n-HA; 0, 5, 10, 15, 20 and 30wt%) were successfully developed by a simple casting/solvent evaporation method. n-HA with size about 20nm in vertical diameter and about 100nm in horizontal diameter was successfully synthesized by a hydro-thermal precipitation method, and then dispersed into chitosan/genipin solution with the aid of continuous ultrasound to develop n-HA/chitosan cross-linking composite membranes. The detailed characterizations including Fourier transform infrared spectroscopy (FTIR), X-ray diffractometer (XRD), thermogravimetric analysis (TGA), scanning electron microscopy (SEM), water adsorption and tensile test were performed....</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376835</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376835</guid>        </item>
        <item>
            <title>Balanced electrostatic blending approach - An alternative to chemical crosslinking of Thai silk fibroin/gelatin scaffold.</title>
            <link>http://www.medworm.com/index.php?rid=5376834&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21983026%26dopt%3DAbstract</link>
            <description>Authors: Jetbumpenkul P, Amornsudthiwat P, Kanokpanont S, Damrongsakkul S
    Abstract
    In tissue engineering, chemical crosslinking is widely used for conjugating two or more biomaterials to mainly control biodegradability and strength. For example, Thai silk fibroin/gelatin scaffold will offer mechanical strength from Thai silk fibroin and cell attraction from gelatin. However, chemical crosslinking requires crosslinking agent which could potentially pose negative impact from remaining trace amount of chemicals especially in medical application. Here we present an alternative approach to chemical crosslinking-a balance electrostatic blending approach. In this approach, two opposite charge biomaterials were selected for blending, with different ratios. Both materials were bound togethe...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376834</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376834</guid>        </item>
        <item>
            <title>Anti-fatigue activity of polysaccharides extract from Radix Rehmanniae Preparata.</title>
            <link>http://www.medworm.com/index.php?rid=5376833&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21983027%26dopt%3DAbstract</link>
            <description>Authors: Tan W, Yu KQ, Liu YY, Ouyang MZ, Yan MH, Luo R, Zhao XS
    Abstract
    The anti-fatigue effects of the Radix Rehmanniae Preparata polysaccharides (RRPP) were studied in mice. The RRPP were orally administered at doses of 50, 100 and 200mg/kg for 4 weeks and the anti-fatigue activity was evaluated using a weight-loaded swimming test, along with the determination of serum urea nitrogen (SUN), hepatic glycogen and blood lactic acid (BLA) contents. The results showed that there was no significant difference in the body weight of mice in the three RRPP groups compared with the negative control group during initial, intermediate and terminal stages in the experiment (p&amp;gt;0.05). The ratio of exhausting swimming time was obviously increased 31.48% (p&amp;lt;0.05) and 61.51% (p&amp;lt;0.01) in ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376833</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376833</guid>        </item>
        <item>
            <title>Protective effects of sulfated chitooligosaccharides against hydrogen peroxide-induced damage in MIN6 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5376832&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21983028%26dopt%3DAbstract</link>
            <description>Authors: Lu X, Guo H, Zhang Y
    Abstract
    Sulfated chitooligosaccharides (COS-S) with different degrees of substitution (DS) were obtained by the chlorosulfuric acid/pyridine method. Protective effects of COS-S against hydrogen peroxide (H(2)O(2))-induced damage were investigated in pancreatic β-cells MIN6 cell line. The cell viability, morphology, insulin contents, malondialdehyde (MDA) inhibition, lactate dehydrogenase (LDH) release and the levels of antioxidant enzymes including catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidise (GPx) were evaluated under oxidative damage by 150μM H(2)O(2) for 6h. COS-S did not show any harmful or inhibitory effect on cell growth at concentrations ranging from 0.1 to 0.5mg/ml. While COS-S could enhance the cell viability, decre...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376832</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376832</guid>        </item>
        <item>
            <title>Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei.</title>
            <link>http://www.medworm.com/index.php?rid=5376831&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21986542%26dopt%3DAbstract</link>
            <description>Authors: Chambergo FS, Valencia EY, Ferreira-Júnior JR, Camilo CM, Campana PT
    Abstract
    Superoxide dismutases (SODs; EC 1.15.1.1) are part of the antioxidant system of aerobic organisms and are used as a defense against oxidative injury caused by reactive oxygen species (ROS). The cloning and sequencing of the 788-bp genomic DNA from Trichoderma reesei strain QM9414 (anamorph of Hypocrea jecorina) revealed an open reading frame encoding a protein of 212 amino acid residues, with 65-90% similarity to manganese superoxide dismutase from other filamentous fungi. The TrMnSOD was purified and shown to be stable from 20 to 90°C for 1h at pH from 8 to 11.5, while maintaining its biological activity.
    PMID: 21986542 [PubMed - as supplied by publisher] (Source: International Journal of ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376831</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376831</guid>        </item>
        <item>
            <title>A new chitosan-thymine conjugate: Synthesis, characterization and biological activity.</title>
            <link>http://www.medworm.com/index.php?rid=5376830&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21986543%26dopt%3DAbstract</link>
            <description>Authors: Kumar S, Kim H, Gupta MK, Dutta PK, Koh J
    Abstract
    Conjugation of chitosan with nucleobases is expected to expand its not only antimicrobial activity but also anti-cancer activity. Here, we report the synthesis of a novel chitosan-thymine conjugate by the reaction between chitosan and thymine-1-yl-acetic acid followed by acylation. The synthesized conjugate was characterized by FTIR, XRD, (1)H NMR, TGA and SEM. The microbiological screening results demonstrated the antimicrobial activity of the conjugate against bacteria viz., Escherichia coli, Staphylococcus aureus, Candida albicans, and fungi viz., Aspergillus niger. The chitosan-thymine conjugate also inhibited (p&amp;lt;0.05) the proliferation of human liver cancer cells (HepG2) in a dose-dependent manner but had no cellul...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376830</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376830</guid>        </item>
        <item>
            <title>The effects of electrolysis at room temperature on retrogradation of sweet potato starch.</title>
            <link>http://www.medworm.com/index.php?rid=5376825&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22008104%26dopt%3DAbstract</link>
            <description>Authors: Xijun L, Kunsheng Z, Qingfeng L, Xu Z, Shuyi Z
    Abstract
    The effects of electrolysis at room temperature on formation of sweet potato retrograded starch were studied by photographic method in the paper. The optimal parameters of electrolytic preparation of sweet potato retrograded starch were determined. The ratio between sweet potato starch and water was 10g/100mL with addition of NaCl 1.0g/100mL, pH value of the solution was 6.0 and the solution was electrolyzed for 30min at 90V at room temperature, then it was stored at 4°C for 24h after being autoclaved for 30min at 120°C, the retrogradation rate of sweet potato starch at this condition was 33.1%, which is 138% higher than that of control group. Four possible reasons are put forward to explain the results.
    PMID: 2...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376825</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376825</guid>        </item>
        <item>
            <title>Chitosan scaffolds containing silicon dioxide and zirconia nano particles for bone tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5294067&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21968009%26dopt%3DAbstract</link>
            <description>Authors: Pattnaik S, Nethala S, Tripathi A, Saravanan S, Moorthi A, Selvamurugan N
    Abstract
    A scaffold harboring the desired features such as biodegradation, biocompatibility, porous structure could serve as template for bone tissue engineering. In the present study, chitosan (CS), nano-scaled silicon dioxide (Si) and zirconia (Zr) were combined by freeze drying technique to fabricate a bio-composite scaffold. The bio-composite scaffold (CS/Si/Zr) was characterized by SEM, XRD and FT-IR studies. The scaffold possessed a porous nature with pore dimensions suitable for cell infiltration and colonization. The presence of zirconia in the CS/Si/Zr scaffold decreased swelling and increased biodegradation, protein adsorption and bio-mineralization properties. The CS/Si/Zr scaffold was als...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294067</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294067</guid>        </item>
        <item>
            <title>A novel glycosaminoglycan-like polysaccharide from abalone Haliotis discus hannai Ino: Purification, structure identification and anticoagulant activity.</title>
            <link>http://www.medworm.com/index.php?rid=5294066&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21968010%26dopt%3DAbstract</link>
            <description>Authors: Li G, Chen S, Wang Y, Xue Y, Chang Y, Li Z, Wang J, Xue C
    Abstract
    A novel glycosaminoglycan-like sulfated polysaccharide (AAP) from the pleopods of Haliotis discus hannai Ino was purified by DEAE ion exchange chromatography followed with S-300 HR geltrion chromatography. Chemical composition analysis indicated that AAP was composed of galactosamine, glucuronic acid, fucose, galactose with a ratio of 2.14:2.37:2.94:1, the content of sulfate was 15.5%. The average molecular weight (M(w)) was 56.2kDa in a TSK G4000 column. Further IR, 1D, 2D NMR spectroscopic analysis of the correlation signals of different sugar units gave a proposal repeating structure, as follows: In vitro anticoagulant assay indicated AAP prolonged both the activated partial thromboplastin time (APTT) an...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294066</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294066</guid>        </item>
        <item>
            <title>Synthesis and evaluation of physicochemical properties of cross-linked sago starch.</title>
            <link>http://www.medworm.com/index.php?rid=5294065&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21971581%26dopt%3DAbstract</link>
            <description>Authors: Singh AV, Nath LK
    Abstract
    Highly substituted sago starch phosphate was synthesized using POCl(3) as cross-linking reagent. Titrimetric and Fourier transform infra red (FT-IR) spectral analysis were used to characterize the substitution. Studying the different factors affecting the reaction parameters showed that the optimal conditions for starch phosphorylation were: 4h reaction time and reagent concentration 3% (w/w). The physicochemical properties of cross-linked sago starch (CLSS) were done using Scanning electron micrograph (SEM), X-ray powder diffractometer (XRD), Thermogravimetric analysis (TGA). The results revealed that crystalline nature of native sago starch was transformed after cross-linking. TGA report exhibited higher thermal stability, which makes it suitab...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294065</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294065</guid>        </item>
        <item>
            <title>Chemical compositions and bioactivities of crude polysaccharides from tea leaves beyond their useful date.</title>
            <link>http://www.medworm.com/index.php?rid=5272859&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21946077%26dopt%3DAbstract</link>
            <description>Authors: Xiao J, Huo J, Jiang H, Yang F
    Abstract
    The chemical compositions and bioactivities of crude tea polysaccharides (TPS) from the out-of-date tea leaves (beyond their useful date), namely Xihu Longjing (XTPS), Anxi Tieguanyin (TTPS), Chawentianxia (CTPS) and Huizhoulvcha (HTPS), in market were investigated. These TPS showed similar neutral sugar content and different distribution of molecular weight (1-800kD). These crude TPS were mainly composed of rhamnose, arabinose, galactose, glucose, xylose, mannose, and galacturonic acid. IR spectra confirmed that these crude TPS were composed of polysaccharide, protein and uronic acids. These TPS showed similar DPPH scavenging activity and exhibited lower DPPH scavenging activities than Vc within 25-200μg/mL. However, these TPS with...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272859</comments>
            <pubDate>Mon, 19 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272859</guid>        </item>
        <item>
            <title>In-situ silica incorporated carboxymethyl tamarind: Development and application of a novel hybrid nanocomposite.</title>
            <link>http://www.medworm.com/index.php?rid=5272858&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21946078%26dopt%3DAbstract</link>
            <description>Authors: Pal S, Gorain MK, Giri A, Bandyopadhyay A, Panda AB
    Abstract
    A novel hybrid nanocomposite has been prepared using in situ incorporation of nano-sized filler (silica) onto carboxymethyl tamarind kernel polysaccharide (CMT). Various characterizations were employed to confirm that silica nano particles have been incorporated onto the polymer matrix. Rheological characteristics revealed stronger CMT-Si interaction at 0.5 and 1wt% level. Beyond 1wt% Si concentration, the interaction is less and so there is little drop in shear viscosity. Flocculation efficiency increases with incorporation of nano filler, maximum efficacy being observed at 1wt% silica concentration. All the nanocomposites exhibited better flocculation characteristics in comparison to pure CMT.
    PMID: 2194607...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272858</comments>
            <pubDate>Mon, 19 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272858</guid>        </item>
        <item>
            <title>Glucose and pH dual-responsive concanavalin A based microhydrogels for insulin delivery.</title>
            <link>http://www.medworm.com/index.php?rid=5272857&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21946079%26dopt%3DAbstract</link>
            <description>Authors: Yin R, Tong Z, Yang D, Nie J
    Abstract
    Glucose and pH dual-responsive microhydrogels based on concanavalin A (Con A) were prepared and used for insulin delivery. The combination of the specific saccharide-binding affinity of Con A and the cationic groups of N-(2-(dimethylamino) ethyl)-methacrylamide (DMAEMA) led to dual-responsive systems. SEM, fluorescence microscopy and particle size analysis showed that the obtained microhydrogels had a dense surface morphology and an average size of 38μm. The in vitro insulin release study revealed that the microhydrogels could quickly respond to the changes of glucose concentrations in the medium and small change in pH value of the environment. The kinetics of insulin release was analyzed by using empirical equation and the apparent d...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272857</comments>
            <pubDate>Mon, 19 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272857</guid>        </item>
        <item>
            <title>Carboxymethylation of polysaccharides from Auricularia auricula and their antioxidant activities in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=5272861&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945678%26dopt%3DAbstract</link>
            <description>Authors: Yang L, Zhao T, Wei H, Zhang M, Zou Y, Mao G, Wu X
    Abstract
    The chemical carboxymethylated polysaccharide (CMAAP), which is derived from the poorly water-soluble, crude polysaccharide from Auricularia auricula (AAP), was prepared. The degree of substitution of CMAAP was 0.857, and its solubility in water reached 0.6mg/mL, much higher than that of AAP (0.1mg/mL). One fraction, CMAAP22, was purified. Chemical analysis indicated that CMAAP22 was composed of mannose and glucose in a ratio of 1.06:1 with a molecular weight of 3.4×10(6)Da. IR spectra and (13)C NMR spectra indicated that the C2, C4 and C6 positions were partially substituted by -CH(2)COOH. AFM revealed that CMAAP22 was spherical particle structure with a diameter of 80-300nm. Moreover, the antioxidant activity o...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272861</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272861</guid>        </item>
        <item>
            <title>Cytotoxicity and mechanical behavior evaluation of chitin-bentonite clay based polyurethane bio-nanocomposites.</title>
            <link>http://www.medworm.com/index.php?rid=5272860&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945787%26dopt%3DAbstract</link>
            <description>Authors: Zia KM, Zuber M, Barikani M, Hussain R, Jamil T, Anjum S
    Abstract
    Chitin based polyurethane bio-nanocomposites (PUBNC) were prepared using chitin, Delite(®) HPS bentonite nanoclay enriched in montmorillonite (MMT), 4,4'-diphenylmethane diisocyanate (MDI) and polycaprolactone polyol CAPA 231 (3000g/mol(-1)). The prepolymers having different concentration of Delite HPS bentonite nanoclay were extended with 2moles of chitin. The structures of the resulted polymers were determined by FT-IR technique. The effect of nanoclay contents on mechanical properties and in vitro biocompatibility was investigated. The mechanical properties of the synthesized materials were improved with increase in the Delite HPS(®) bentonite nanoclay contents. Optimum mechanical properties were obtain...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272860</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272860</guid>        </item>
        <item>
            <title>Free radical scavenging and angiotensin-I converting enzyme inhibitory peptides from Pacific cod (Gadus macrocephalus) skin gelatin.</title>
            <link>http://www.medworm.com/index.php?rid=5272856&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945677%26dopt%3DAbstract</link>
            <description>Authors: Ngo DH, Ryu B, Vo TS, Himaya SW, Wijesekara I, Kim SK
    Abstract
    Potent antioxidative peptides were purified from Pacific cod (Gadus macrocephalus) skin gelatin using alcalase, neutrase, papain, trypsin, pepsin, and α-chymotrypsin. Among them, the papain hydrolysate exhibited the highest antioxidant activity. Therefore, it was further purified and obtained two peptides with amino acid sequences of Thr-Cys-Ser-Pro (388Da) and Thr-Gly-Gly-Gly-Asn-Val (485.5Da). The antioxidant activity of the purified peptides was performed by electron spin resonance technique. Moreover, their intracellular free radical scavenging activity using 2',7'-dichlorofluorescin diacetate and the protective effect against oxidation-induced DNA damage were evaluated in mouse macrophages (RAW 264.7 cell...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272856</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272856</guid>        </item>
        <item>
            <title>Variability of cell wall polysaccharides composition and hemicellulose enzymatic profile in an apple progeny.</title>
            <link>http://www.medworm.com/index.php?rid=5257359&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21939685%26dopt%3DAbstract</link>
            <description>Authors: Galvez-Lopez D, Laurens F, Quéméner B, Lahaye M
    Abstract
    The genetic variability of apple cell walls polysaccharides chemical composition and structure was assessed in a progeny of 141 individuals harvested over 2 years. The variability of the hemicelluloses oligosaccharides released by glucanase was analyzed by MALDI-TOF MS. The genetic contribution was distinguished from harvest year as well as from parental crossing patterns and scab resistance selection. Results showed that harvest year had a major impact on cell wall polysaccharide composition and structure. Within each harvest, genetic effect impact more significantly cell wall polysaccharide chemistry than does reciprocal crossing or early scab selection. Uronic acids, glucose, galactose and xylose contents as wel...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5257359</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5257359</guid>        </item>
        <item>
            <title>Electrochemical spectroscopic investigations on the interaction of an ytterbium complex with DNA and their analytical applications such as biosensor.</title>
            <link>http://www.medworm.com/index.php?rid=5257358&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21939686%26dopt%3DAbstract</link>
            <description>Authors: Ilkhani H, Ganjali MR, Arvand M, Hejazi MS, Azimi F, Norouzi P
    Abstract
    Metal ion-DNA interactions are important in nature, often changing the genetic material's structure and function. A new Yb complex of YbCl(3) (tris(8-hydroxyquinoline-5-sulfonic acid) ytterbium) was synthesized and utilized as an electrochemical indicator for the detection of DNA oligonucleotide based on its interaction with Yb(QS)(3). Cyclic voltammetry (CV) and fluorescence spectroscopy were used to investigate the interaction of Yb(QS)(3) with ds-DNA. It was revealed that Yb(QS)(3) presented an excellent electrochemical activity on glassy carbon electrode (GCE) and could intercalate into the double helix of double-stranded DNA (ds-DNA). The binding mechanism of interaction was elucidated on glassy c...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5257358</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5257358</guid>        </item>
        <item>
            <title>A cytotoxic type-2 ribosome inactivating protein (from leafless mistletoe) lacking sugar binding activity.</title>
            <link>http://www.medworm.com/index.php?rid=5240785&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21930153%26dopt%3DAbstract</link>
            <description>Authors: Das MK, Sharma RS, Mishra V
    Abstract
    Articulatin-D, a 66kDa ribosome inactivating protein (RIP) comprised of 29kDa A-chain linked to 35kDa B-chain, is purified from leafless mistletoe (Viscum articulatum) parasitic on Dalbergia sp. from Western Ghats (India). N-terminal sequence and LC-MS/MS analyses of A- and B-chain confirmed that articulatin-D is a type-2 RIP having high homology with other mistletoe lectins. Translation inhibition and diagnostic N-glycosidase activity of articulatin-D illustrate the presence of catalytically active A-chain. Its inability to: (i) bind to acid treated Sepharose CL-6B column, (ii) agglutinate trypsin-treated and untreated RBCs of human (A, B, O, AB), mice, rat, rabbit, buffalo, porcine, pigeon, cock, fish, sheep and goat even with 10mg/ml...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240785</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240785</guid>        </item>
        <item>
            <title>Chemical analysis and antioxidant activity in vitro of polysaccharides extracted from Boletus edulis.</title>
            <link>http://www.medworm.com/index.php?rid=5240784&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21930154%26dopt%3DAbstract</link>
            <description>In this study, three crude polysaccharides (BEPF30, BEPF60 and BEPF80) were isolated from the fruiting bodies of B. edulis with boiling water. Chemical and physical characteristics of the three crude polysaccharides were investigated by the combination of chemical and instrumental analysis methods. Their antioxidant activities were investigated in vitro systems including hydroxyl assay, superoxide radical assay, reducing power and chelating activity. Among these three polysaccharides, BEPF60 showed more significant reducing power and chelating activity; and highest inhibitory effects on superoxide radical and hydroxyl radical. These results indicated that polysaccharides extracted from B. edulis might be employed as ingredients in healthy and functional food to alleviate the oxidative stre...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240784</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240784</guid>        </item>
        <item>
            <title>Synthesis of oxidized guar gum by dry method and its application in reactive dye printing.</title>
            <link>http://www.medworm.com/index.php?rid=5240789&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925204%26dopt%3DAbstract</link>
            <description>Authors: Gong H, Liu M, Zhang B, Cui D, Gao C, Ni B, Chen J
    Abstract
    The aim of this study was to prepare oxidized guar gum with a simple dry method, basing on guar gum, hydrogen peroxide and a small amount of solvent. To obtain a product with suitable viscosity for reactive dye printing, the effects of various factors such as the amount of oxidant and solvent, reaction temperature and time were studied with respect to the viscosity of reaction products. The product was characterized by Fourier transform infrared spectroscopy, size exclusion chromatography, scanning electron microscopy and differential scanning calorimetry. The hydrated rate of guar gum and oxidized guar gum was estimated through measuring the required time when their solutions (1%, w/v) reached the maximum viscosi...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240789</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240789</guid>        </item>
        <item>
            <title>Oral administration of levan polysaccharide reduces the alloxan-induced oxidative stress in rats.</title>
            <link>http://www.medworm.com/index.php?rid=5240787&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925206%26dopt%3DAbstract</link>
            <description>This study aimed to evaluate the effect of a polysaccharide named levan, which was produced by new isolated bacteria, on oxidative stress and hyperglycemia in alloxan-induced diabetic rats. Levan polysaccharide was given in drinking water for 60 days at a daily dose equivalent to 2%. The oral administration of levan in diabetic rats caused a decrease in glucose level in plasma and an increase of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) activities in both pancreas and liver. Furthermore, a protective action against hepatic and pancreatic toxicity in diabetic rats was clearly observed. Furthermore, a significant decrease in hepatic and pancreatic indices toxicity was observed, i.e., alkalines phosphatases (ALP), aspartate and lactate transaminases (AST and ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240787</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240787</guid>        </item>
        <item>
            <title>Molecular dynamics study of the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius.</title>
            <link>http://www.medworm.com/index.php?rid=5240786&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925536%26dopt%3DAbstract</link>
            <description>Authors: Pagano B, Del Vecchio P, Mattia CA, Graziano G
    Abstract
    Circular dichroism and differential scanning calorimetry measurements showed that esterase 2 from the thermophilic microorganism Alicyclobacillus acidocaldarius, EST2, and its variant in which the first 35 residues have been deleted, EST2-36del, unfold reversibly on increasing temperature, and possess two cooperative and coupled domains [12]. Structural features of the α/β hydrolase fold of EST2, with nine α-helices packed against the central twisted β-sheet, do not allow a straightforward identification of these two cooperative and coupled domains. Molecular dynamics simulations, each one 20ns long, have been performed at 300, 400 and 500K, on both proteins in explicit water. Suitable analysis of MD trajectories ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240786</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240786</guid>        </item>
        <item>
            <title>Jack bean α-mannosidase (Jbα-man): Tolerance to alkali, chelating and reducing agents and energetics of catalysis and inhibition.</title>
            <link>http://www.medworm.com/index.php?rid=5240790&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21924285%26dopt%3DAbstract</link>
            <description>Authors: Kumar A, Gaikwad SM
    Abstract
    Investigations of the catalytic and structural transitions of jack bean α-mannosidase (Jbα-man) are described in the present paper. The enzyme was maximally stable at pH 5.0; however, when incubated in the pH range of 11.0-12.0, showed 1.3 times higher activity and also stability for longer time. The free amino group at or near the active site was probably involved in the stability and activation mechanism. The active site is constituted by the association of two unidentical subunits connected by disulfide linkages. The metalloenzyme has Zn(2+) ions tightly bound and chelation reduces the thermal stability of the protein. Energetics of catalysis and thermodynamics of inhibition of the enzyme were also carried out.
    PMID: 21924285 [PubMed -...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240790</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240790</guid>        </item>
        <item>
            <title>Suicide inactivation of peroxidase from Chamaerops excelsa palm tree leaves.</title>
            <link>http://www.medworm.com/index.php?rid=5240788&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925205%26dopt%3DAbstract</link>
            <description>Authors: Cuadrado NH, Zhadan GG, Roig MG, Shnyrov VL
    Abstract
    The concentration and time-dependences and the mechanism of the inactivation of Chamaerops excelsa peroxidase (CEP) by hydrogen peroxide were studied kinetically with four co-substrates (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), guaiacol, o-dianisidine and o-phenylenediamine). The turnover number (r) of H(2)O(2) required to complete the inactivation of the enzyme varied for the different substrates, the enzyme most resistant to inactivation (r=4844) with ABTS being the most useful substrate for biotechnological applications, opening a new avenue of enquiry with this peroxidase.
    PMID: 21925205 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240788</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240788</guid>        </item>
        <item>
            <title>Synthesis and in vitro studies of biodegradable modified chitosan nanoparticles for photodynamic treatment of cancer.</title>
            <link>http://www.medworm.com/index.php?rid=5215668&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907233%26dopt%3DAbstract</link>
            <description>Authors: Reza Saboktakin M, Tabatabaie RM, Maharramov A, Ali Ramazanov M
    Abstract
    The main aim of this research is to study the in vitro photocytotoxicity and cellular uptake of biodegradable polymeric nanoparticles loaded with photosensitizer mTHPP. As the first part of a continued research on conversion of N-sulfonato-N,O-carboxymethylchitosan (NOCCS) to useful biopolymer-based materials, large numbers of carboxylic functional groups were introduced onto NOCCS by grafting with polymethacrylic acid (PMAA). The free radical graft copolymerization was carried out at 70°C, bis-acrylamide as a cross-linking agent and persulfate as an initiator. These results show that the nanoparticles have high loading capacity and stability. These nanoparticles are suitable as carriers for photodyn...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215668</comments>
            <pubDate>Fri, 02 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215668</guid>        </item>
        <item>
            <title>In vitro and in vivo immunomodulatory activity of sulfated polysaccharides from Enteromorpha prolifera.</title>
            <link>http://www.medworm.com/index.php?rid=5215666&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907732%26dopt%3DAbstract</link>
            <description>Authors: Kim JK, Cho ML, Karnjanapratum S, Shin IS, You SG
    Abstract
    Water-soluble sulfated polysaccharides extracted from Enteromorpha prolifera and fractionated using ion-exchange chromatography (crude, F(1), F(2) and F(3) fractions) were investigated to determine their in vitro and in vivo immunomodulatory activities. The sulfated polysaccharides, especially the F(1) and F(2) fractions, stimulated a macrophage cell line, Raw 264.7, inducing considerable nitric oxide (NO) and various cytokine production via up-regulated mRNA expression. The in vivo experiment results show that the sulfated polysaccharides (the crude and F(2) fractions) significantly increased Con A-induced splenocyte proliferation, revealing their potential comitogenic activity. In addition, IFN-γ and IL-2 secret...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215666</comments>
            <pubDate>Fri, 02 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215666</guid>        </item>
        <item>
            <title>In vitro antioxidant activities of sulfated polysaccharide fractions extracted from Corallina officinalis.</title>
            <link>http://www.medworm.com/index.php?rid=5215672&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21896282%26dopt%3DAbstract</link>
            <description>Authors: Yang Y, Liu D, Wu J, Chen Y, Wang S
    Abstract
    Sulfated polysaccharides (F1, F2) from seaweed Corallina officinalis were isolated through anion-exchange column chromatography. Their chemical characteristics were determined by GC, HPLC, FT-IR and UV spectra. F1 and F2 contained only two monosaccharides, namely galactose and xylose. The antioxidant activities of F1, F2 and the de-sulfated polysaccharides (DF-1, DF-2) in vitro were investigated, including hydroxyl radicals scavenging effect, superoxide radical scavenging capacity, DPPH radical activity and reducing power. As expected, antioxidant assay showed that the two sulfated polysaccharide fractions (F1, F2) possessed considerable antioxidant properties and had more excellent abilities than de-sulfated polysaccharides (DF...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215672</comments>
            <pubDate>Thu, 01 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215672</guid>        </item>
        <item>
            <title>Influence of viscous Rhodella grisea (Rhodophyceae) proteoglycan on chemically induced cough reflex.</title>
            <link>http://www.medworm.com/index.php?rid=5215669&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21906620%26dopt%3DAbstract</link>
            <description>Authors: Nosáľová G, Capek P, Flešková D, Jureček L, Hindák F, Lukavský J, Cepák V, Ray B, Breierová E, Turjan J
    Abstract
    An algal extracellular biopolymer (over 8.5×10(5)Da) composed of carbohydrates (52%) and protein (∼13%) has been isolated from a red alga Rhodella grisea growing in natural conditions by concentration of water medium, alcohol precipitation, dialysis and freeze-drying. This mucilagineous biopolymer contained xylose and its 3-O- and 4-O-methyl derivatives (∼63%), galactose (∼12%), glucuronic acid (11-12%), glucose (∼5%), rhamnose (∼4%), fucose (∼3-4%) and low content of others accompaning sugars. When tested on the citric acid-induced cough and reactivity of airways smooth muscle in vivo in the test system guinea pigs, this biopolymer assign...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215669</comments>
            <pubDate>Thu, 01 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215669</guid>        </item>
        <item>
            <title>An analysis of temperature adaptation in cold active, mesophilic and thermophilic Bacillus α-amylases.</title>
            <link>http://www.medworm.com/index.php?rid=5215667&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907234%26dopt%3DAbstract</link>
            <description>Authors: Mahdavi A, Sajedi RH, Asghari SM, Taghdir M, Rassa M
    Abstract
    A comparative biochemical and structural study was performed on a cold active α-amylase from Bacillus cereus (BCA) and two well-known homologous mesophilic and thermophilic α-amylases from Bacillus amyloliquefaciens (BAA) and Bacillus licheniformis (BLA). In spite of a high degree of sequence and structural similarity, drastic variations were found for T(opt) as 50, 70 and 90°C for BCA, BAA and BLA, respectively. The half-lives of thermoinactivation were 1 and 9min for BCA and BAA at 80°C respectively, whilst there was no inactivation for BLA at this temperature. Thermodynamic studies on inactivation process suggested that lower thermostability of BCA is due to lower inactivation slope of the Arrhenius plots...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215667</comments>
            <pubDate>Thu, 01 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215667</guid>        </item>
        <item>
            <title>Sugarcane Hsp101 is a hexameric chaperone that binds nucleotides.</title>
            <link>http://www.medworm.com/index.php?rid=5215670&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21903129%26dopt%3DAbstract</link>
            <description>Authors: Cagliari TC, da Silva VC, Borges JC, Prando A, Tasic L, Ramos CH
    Abstract
    The Clp/Hsp100 AAA+ chaperone family is involved in recovering aggregated proteins and little is known about other orthologs of the well studied ClpB from Escherichia coli and Hsp104 from Saccharomyces cerevisiae. Plant Hsp101 is a good model for understanding the relationship between the structure and function of Hsp100 proteins and to investigate the role of these chaperones in disaggregation processes. Here, we present the cloning and purification of a sugarcane ortholog, SHsp101, which is expressed in sugarcane cells and is a folded hexamer that is capable of binding nucleotides. Thus SHsp101 has the structural and functional characteristics of the Clp/Hsp100 AAA+ family.
    PMID: 21903129 [PubM...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215670</comments>
            <pubDate>Wed, 31 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215670</guid>        </item>
        <item>
            <title>Aromatic interactions at atom-to-atom contact and just beyond: A case study of protein interactions of NAD(+)/NADP(+).</title>
            <link>http://www.medworm.com/index.php?rid=5215671&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21903128%26dopt%3DAbstract</link>
            <description>Authors: Gupta P, Durani S
    Abstract
    We probed aromatic-protein interactions based on specificity of enrichment of protein residues across a contact-based cutoff. Thus, 155 protein-NAD(+)/NADP(+) complexes were analyzed for enrichments within 10Å of centroids of aromatic groups of the ligand when the residues were contacted and not contacted with the aromatic ligand. Specifically, neutral-adenine and cationic-nicotinamide groups of the oxidized coenzymes evoked interest to know whether the contrast of charge or the shared aromaticity will manifest in the enrichments across the cutoff. We found that when in contact, the enrichments are highly specific for nicotinamide and adenine-aromatic structures, and thus possibly complex in the basis, but when not in contact, they are generic ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215671</comments>
            <pubDate>Tue, 30 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215671</guid>        </item>
        <item>
            <title>Purification and physicochemical properties of different polysaccharide fractions from the water extract of Boschniakia rossica and their effect on macrophages activation.</title>
            <link>http://www.medworm.com/index.php?rid=5215675&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21893087%26dopt%3DAbstract</link>
            <description>Authors: Liu Y, Sheng Y, Yuan G, Wang Y, Wei H, Guan M, Pei J
    Abstract
    Today more and more attentions had been attracted by many nutritionists and pharmacologists on polysaccharides from natural plants or animals due to their significant biological activities. In this research three polysaccharides (BRR-W1, BRR-WA1 and BRR-WA2) were isolated and purified from the water extract of Boschniakia rossica by DEAE Sepharose Fast Flow and Sepharose 6 Fast Flow column chromatography. Chemical and physical characteristics of three polysaccharides were investigated by a combination of chemical and instrumental analysis methods. The assays of their effect on macrophages activation were also investigated in vitro, including phagocytosis of macrophages, detections for NO production and TNF-α se...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215675</comments>
            <pubDate>Sat, 27 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215675</guid>        </item>
        <item>
            <title>A facile method for preparing biodegradable chitosan derivatives with low grafting degree of poly(lactic acid).</title>
            <link>http://www.medworm.com/index.php?rid=5215674&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21893088%26dopt%3DAbstract</link>
            <description>Authors: Li J, Kong M, Cheng XJ, Li JJ, Liu WF, Chen XG
    Abstract
    Chemical modification of chitosan by grafting with PLA (CS-g-PLA) was developed via 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) mediated coupling reaction. The introduction of PLA disrupted the crystalline structure of chitosan, improved its solubility and thermal stability. Low degree of PLA substitution showed better degradation efficiency than chitosan and PLA. Weight loss of CS-g-PLA6 and CS-g-PLA4 was 87% and 94%, respectively, in 7 days enzymatic degradation study. CS-g-PLA2 was totally degraded in 1 day. Self-assembly behavior was studied using pyrene fluorescence dye technique and found to be PLA grafting level dependent. CS-g-PLA with low grafting degree showed hydrophilic, self-assembling properties...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215674</comments>
            <pubDate>Sat, 27 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215674</guid>        </item>
        <item>
            <title>Synthesized oversulfated and acetylated derivatives of polysaccharide extracted from Enteromorpha linza and their potential antioxidant activity.</title>
            <link>http://www.medworm.com/index.php?rid=5215673&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21893089%26dopt%3DAbstract</link>
            <description>Authors: Zhang Z, Wang X, Yu S, Yin L, Zhao M, Han Z
    Abstract
    Sulfated polysaccharide extracted from blue algae Enteromorpha linza is proved to possess excellent antioxidant activities. Two derivatives by means of oversulfated and acetylated coupling were synthesized and investigated their antioxidant activities including scavenging effect of superoxide, hydroxyl and 1,1-diphenyl-2-picrylhydrazyl radicals. And then the relationship between antioxidant activity and chemical characteristics was characterized. The results of chemical analysis and FT-IR showed that the modification of polysaccharide was successful. In addition, it was found that certain derivatives exhibited stronger antioxidant activity than raw material. They could serve as free-radical inhibitors or scavengers, acti...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215673</comments>
            <pubDate>Sat, 27 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215673</guid>        </item>
        <item>
            <title>Formulation optimization of chelerythrine loaded O-carboxymethylchitosan microspheres using response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=5215681&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889529%26dopt%3DAbstract</link>
            <description>Authors: Li GY, Zhong M, Zhou ZD, Zhong YD, Ding P, Huang Y
    Abstract
    The aims of this investigation were to develop a procedure to prepare chelerythrine (CHE) loaded O-carboxymethylchitosan (O-CMCS) microspheres by emulsion cross-linking method and optimize the process and formulation variables using response surface methodology (RSM) with a three-level, three-factor Box-Behnken design (BBD). The independent variables studied were O-CMCS/CHE ratio, O/W phase ratio, and O-CMCS concentration, dependent variables (responses) were drug loading content and encapsulation efficiency. Mathematical equations and response surface plots were used to relate the dependent and independent variables. The process and formulation variables were optimized to achieve maximum drug loading content and ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215681</comments>
            <pubDate>Fri, 26 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215681</guid>        </item>
        <item>
            <title>Encapsulation of probiotic Bifidobacterium longum BIOMA 5920 with alginate-human-like collagen and evaluation of survival in simulated gastrointestinal conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5215680&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889530%26dopt%3DAbstract</link>
            <description>Authors: Su R, Zhu XL, Fan DD, Mi Y, Yang CY, Jia X
    Abstract
    Alginate (ALg)-human-like collagen (HLC) microspheres were prepared by the technology of electrostatic droplet generation in order to develop a biocompatible vehicle for probiotic bacteria. Microparticles were spherical with mean particle size of 400μm. The encapsulation efficiency (EE) of ALg-HLC microspheres could reach 92-99.2%. Water-soluble and fibrous human-like collagen is combined with sodium alginate through intermolecular hydrogen bonding and electrostatic force which were investigated by Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC), thus the matrix of ALg-HLC was very stable. Bifidobacterium longum BIOMA 5920, as a kind of probiotic bacteria, was encapsulated with ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215680</comments>
            <pubDate>Fri, 26 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215680</guid>        </item>
        <item>
            <title>Molecular characterization and solution properties of enzymatically tailored arabinoxylans.</title>
            <link>http://www.medworm.com/index.php?rid=5215679&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889531%26dopt%3DAbstract</link>
            <description>In this study, we noticed that not only the arabinose-to-xylose ratio but also the position of the arabinofuranosyl substituents affects the water-solubility of arabinoxylans. The AXH-d3 treatment had no significant effect on the solution conformation of arabinoxylans, but the density of the arabinoxylan molecules decreased in DMSO solution after AXH-m modification. The possible heterogeneity of arabinoxylans complicated the interpretation of data describing the macromolecular properties of the enzymatically modified samples.
    PMID: 21889531 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215679</comments>
            <pubDate>Fri, 26 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215679</guid>        </item>
        <item>
            <title>X-ray structure of a galactose-specific lectin from Spatholobous parviflorous.</title>
            <link>http://www.medworm.com/index.php?rid=5215678&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889532%26dopt%3DAbstract</link>
            <description>Authors: Geethanandan K, Abhilash J, Bharath SR, Sadasivan C, Haridas M
    Abstract
    A galactose-specific seed lectin from Spatholobous parviflorus (SPL) has been purified, crystallized and its X-ray structure solved. It is the first lectin purified and crystallized from the genus Spatholobus (family: Fabaceae). The crystals belong to the space group P1, with a=60.792Å, b=60.998Å, c=78.179Å, α=78.68°, β=88.62°, γ=104.32°. The data were collected at 2.04Å resolution under cryocondition, on a MAR image-plate detector system, mounted on a rotating anode X-ray generator. The coordinates of Dolichos biflorus lectin (1lu1) were successfully used for the structure solution by molecular replacement method. The primary structure of the SPL was not known earlier and it was unambigu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215678</comments>
            <pubDate>Fri, 26 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215678</guid>        </item>
        <item>
            <title>Mechanism of inhibition of arginine kinase by flavonoids consistent with thermodynamics of docking simulation.</title>
            <link>http://www.medworm.com/index.php?rid=5215676&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889534%26dopt%3DAbstract</link>
            <description>In this study, two members of the flavonoid family, quercetin (QU) and luteolin (LU), were identified as novel noncompetitive inhibitors of locust arginine kinase. They were found to have inhibition parameters (K(i)) of 11.2 and 23.9μM, respectively. By comparing changes in the activity and intrinsic fluorescence of AK, the inhibition mechanisms of these flavonoids were found to involve binding to Trp residues in the active site. This was determined by examination of the static quenching parameter K(sv). The main binding forces between flavonoids and AK were found to be hydrophobic based on the thermodynamic parameters of changes in enthalpy (ΔH), entropy (ΔS), and free energy (ΔG) and on docking simulation results. Molecular docking analyses also suggested that flavonoids could bind t...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215676</comments>
            <pubDate>Fri, 26 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215676</guid>        </item>
        <item>
            <title>Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein.</title>
            <link>http://www.medworm.com/index.php?rid=5215677&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21889533%26dopt%3DAbstract</link>
            <description>In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.
    PMID: 21889533 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215677</comments>
            <pubDate>Thu, 25 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215677</guid>        </item>
        <item>
            <title>Production of a novel biomacromolecule for nanodevices from glycerol as carbon source in different conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5188992&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871483%26dopt%3DAbstract</link>
            <description>In conclusion, halophilic microorganism Haloarcula sp. IRU1 could be a potential microorganism for production of cruxrhodopsin from glycerol in different conditions.
    PMID: 21871483 [PubMed - as supplied by publisher] (Source: International Journal of Biological Macromolecules)</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188992</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188992</guid>        </item>
        <item>
            <title>Optimization of polysaccharides extraction from Tetrastigma hemsleyanum Diels et Gilg using response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=5188991&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871484%26dopt%3DAbstract</link>
            <description>Authors: Shao Q, Deng Y, Shen H, Fang H, Zhao X
    Abstract
    A 15-run Box-Behnken design (BBD) was used to optimize the extraction conditions of polysaccharides from Tetrastigma hemsleyanum Diels et Gilg. Three factors such as extraction temperature (°C), extraction time (h), and ratio of water to raw material were investigated. The experimental data were fitted to a second-order polynomial equation using multiple regression analysis and also examined using the appropriate statistical methods. The adjusted coefficient of determination (R(Adj)(2)) for the model was 0.9754, and the probability value (P=0.001) demonstrated a high significance for the regression model. The optimum extraction conditions were found to be: optimized extraction temperature 83.3°C, extraction time 1.55h and r...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188991</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188991</guid>        </item>
        <item>
            <title>Immobilization and stabilization of α-galactosidase on Sepabeads EC-EA and EC-HA.</title>
            <link>http://www.medworm.com/index.php?rid=5188988&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871914%26dopt%3DAbstract</link>
            <description>Authors: Bayraktar H, Serilmez M, Karkaş T, Celem EB, Onal S
    Abstract
    α-Galactosidase from tomato has been immobilized on Sepabead EC-EA and Sepabead EC-HA, which were activated with ethylendiamino and hexamethylenediamino groups, respectively. Two strategy was used for the covalent immobilization of α-galactosidase on the aminated Sepabeads: covalent immobilization of enzyme on glutaraldehyde activated support and cross-linking of the adsorbed enzymes on to the support with glutaraldehyde. By using these two methods, all the immobilized enzymes retained very high activity and the stability of the enzyme was also improved. The obtained results showed that, the most stable immobilized α-galactosidase was obtained with the second strategy. The immobilized enzymes were characteriz...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188988</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188988</guid>        </item>
        <item>
            <title>Photocrosslinkable biodegradable responsive hydrogels as drug delivery systems.</title>
            <link>http://www.medworm.com/index.php?rid=5188983&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871915%26dopt%3DAbstract</link>
            <description>Authors: Almeida JF, Ferreira P, Lopes A, Gil MH
    Abstract
    Recently, controlled release from biocompatible materials has received much attention for biomedical applications. Due to their biocompatibility and biodegradability, glucopyranosides such as dextran appear as promising polymeric materials if one is able to regulate their rheological properties and the encapsulation/release efficiency. In this work graft polymer hydrogels from dextran and N-isopropylacrylamide (NIPAAm) were prepared and characterized. Dextran molecules were modified with 2-isocyanatoethylmethacrylate (IEMA) in order to obtain a polymer with carbon double bonds. Urethane linkages resulted from the reaction between hydroxyl groups (OH) of the dextran and isocyanate groups (NCO) of the IEMA. The obtained polyme...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188983</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188983</guid>        </item>
        <item>
            <title>Nano Pd(0) supported on cellulose: A highly efficient and recyclable heterogeneous catalyst for the Suzuki coupling and aerobic oxidation of benzyl alcohols under liquid phase catalysis.</title>
            <link>http://www.medworm.com/index.php?rid=5188982&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871916%26dopt%3DAbstract</link>
            <description>Authors: Jamwal N, Sodhi RK, Gupta P, Paul S
    Abstract
    Nano palladium(0) supported on cellulose was found to be highly efficient recyclable heterogeneous catalyst for the Suzuki coupling between aryl bromides and phenyl boronic acid in water and aerobic oxidation of benzyl alcohols using air as the source of molecular oxygen in acetonitrile. The Cell-Pd(0) was prepared by stirring commercially available cellulose with Pd(OAc)(2) in ethanol at 25°C followed by reduction with hydrazine hydrate, leading finally to nano Pd(0) particles uniformly distributed on surface of cellulose. This catalytic system provides biaryls and polyaryls in excellent yields with very high turn over numbers via Suzuki coupling; and benzaldehyde derivatives in high yields and selectivity by oxidation in air....</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188982</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188982</guid>        </item>
        <item>
            <title>Influence of stabilizers cosolutes on catalase conformation.</title>
            <link>http://www.medworm.com/index.php?rid=5188981&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871917%26dopt%3DAbstract</link>
            <description>Authors: Belluzo S, Boeris V, Farruggia B, Picó G
    Abstract
    The effects of sucrose, mannitol and betaine on the thermodynamic stability and the conformational state of the catalase enzyme were analyzed in order to understand the molecular mechanism whereby the solutes stabilized the enzyme. Catalase was selected as the model enzyme because it is used in several biotechnological processes. In the presence of each cosolute, our data have shown that there was a significant increase in the thermal stability of catalase. A minor stabilization in the enzyme secondary structure were induced by these cosolutes, as circular dichroism in the far UV region has demonstrated. Furthermore, our results support the idea that the overall native structure of catalase becomes more rigid, at least in ...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5188981</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5188981</guid>        </item>
        <item>
            <title>Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent.</title>
            <link>http://www.medworm.com/index.php?rid=5171232&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21856329%26dopt%3DAbstract</link>
            <description>Authors: Zhang M, Wu K, Li G
    Abstract
    The effect of crosslinking agent on pepsin-soluble bovine collagen solution was examined using N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinker. Electrophoretic patterns indicated that crosslinks formed when NHS-AA was added. A higher polarity level deduced from the changes in the fluorescence emission spectrum of pyrene in the crosslinked collagen solution indicated that the formation of well-ordered aggregates was suppressed. The random aggregation of collagens was also observed by atomic force microscopy (AFM). Furthermore, the association of collagens into fibrils was influenced by crosslinking. Self-assembly was suppressed at 37°C; however, as temperature was increased to 39°C, a small amount of NHS-AA leaded to an im...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171232</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171232</guid>        </item>
        <item>
            <title>Immobilization of rat brain acetylcholinesterase on porous gold-nanoparticle-CaCO(3) hybrid material modified Au electrode for detection of organophosphorous insecticides.</title>
            <link>http://www.medworm.com/index.php?rid=5171231&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21856330%26dopt%3DAbstract</link>
            <description>Authors: Chauhan N, Narang J, Pundir CS
    Abstract
    An acetylcholinesterase (AChE) purified from rat brain was immobilized onto gold nanoparticles (AuNPs) assembled on the surface of porous calcium carbonate (CaCO(3)) microsphere. The resulting AChE-AuNPs-CaCO(3) bioconjugate was mounted on the surface of Au electrode with the help of silica sol-gel matrix to prepare the working electrode. This electrode was connected to Ag/AgCl (3M/saturated KCl) as standard and Pt wire as an auxiliary electrode through a potentiostat to construct an organophosphorus (OP) biosensor. The biosensor was based on inhibition of AChE by OP compounds/insecticides. The biosensor showed optimum response at pH 7.0, 30°C, when polarized at +0.2V. Two OP compounds, malathion and chlorpyrifos could be detected i...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171231</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171231</guid>        </item>
        <item>
            <title>Comparative analysis of malate synthase G from Mycobacterium tuberculosis and E. coli: Role of ionic interaction in modulation of structural and functional properties.</title>
            <link>http://www.medworm.com/index.php?rid=5171230&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864568%26dopt%3DAbstract</link>
            <description>Authors: Kumar R, Bhakuni V
    Abstract
    Metabolic plasticity of Mycobacterium renders high degree of adaptive advantages in the persistence through the upregulation of glyoxylate shunt. The malate synthase (MS), an important enzyme of the shunt belongs to the G isoform and expressed predominantly as monomer. Here we did a comparative unfolding studies of two homologous MS from Mycobacterium tuberculosis (MtbMS) and Escherichia coli (ecMS) using various biophysical techniques. Despite having high sequence identities, they show different structural, stability and functional properties. The study suggests that the differences in the stability and unfolding of the two enzymes are by virtue of differential electrostatic modulation unique to their respective molecular assembly.
    PMID: 21...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171230</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171230</guid>        </item>
        <item>
            <title>Hydrogen peroxide targets the cysteine at the active site and irreversibly inactivates creatine kinase.</title>
            <link>http://www.medworm.com/index.php?rid=5171241&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21854802%26dopt%3DAbstract</link>
            <description>Authors: Li C, Sun S, Park D, Jeong HO, Chung HY, Liu XX, Zhou HM
    Abstract
    In our study, we showed that at a relatively low concentration, H(2)O(2) can irreversibly inactivate the human brain type of creatine kinase (HBCK) and that HBCK is inactivated in an H(2)O(2) concentration-dependent manner. HBCK is completely inactivated when incubated with 2mM H(2)O(2) for 1h (pH 8.0, 25°C). Inactivation of HBCK is a two-stage process with a fast stage (k(1)=0.050±0.002min(-1)) and a slow (k(2)=0.022±0.003min(-1)) stage. HBCK inactivation by H(2)O(2) was affected by pH and therefore we determined the pH profile of HBCK inactivation by H(2)O(2). H(2)O(2)-induced inactivation could not be recovered by reducing agents such as dl-dithiothreitol, N-acetyl-l-cysteine, and l-glutathione reduced...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171241</comments>
            <pubDate>Wed, 10 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171241</guid>        </item>
        <item>
            <title>1,3-β-Glucanase from Vigna aconitifolia and its possible use in enzyme bioreactor fabrication.</title>
            <link>http://www.medworm.com/index.php?rid=5171236&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21855566%26dopt%3DAbstract</link>
            <description>Authors: Kestwal RM, Bagal-Kestwal D, Chiang BH
    Abstract
    Endo-1,3(4)-β-glucanase (EC 3.2.1.6) from Vigna aconitifolia sprouts was purified to 14.5 fold by gel filtration and ion-exchange chromatography. The enzyme was found to be a glycoprotein, its activity was Ca(2+) dependent and specific for β-1,3 linkages in different polysaccharides. The K(m) value of the enzyme was estimated to be 3.0mgml(-1) for β-d-glucan as substrate. Circular dichroism studies revealed 8% α-helix, 48% β-pleated and 44% random coil in its secondary structure. Purified β-glucanase was then successfully co-immobilized with glucose oxidase in agarose-chitosan beads, showing better immobilization yield, operational range and stability as compared with the crude β-glucanase beads. The immobilized β-glu...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171236</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171236</guid>        </item>
        <item>
            <title>The building block structure of barley amylopectin.</title>
            <link>http://www.medworm.com/index.php?rid=5171234&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21855567%26dopt%3DAbstract</link>
            <description>This study investigated the building block structure of domains (groups of clusters) and clusters in four different barley genotypes. Two of the barleys possessed the amo1 mutation, Glacier Ac38 and the double recessive SW 49427 with both wax and amo1 mutations, and were compared with the two waxy-type barleys Cinnamon and Cindy. A previous detailed study on these four barley genotypes showed that the amo1 mutation affected the internal structure of amylopectin as manifested in the composition of clusters. In this work the building blocks were isolated from domains and clusters by extensive treatment with liquefying α-amylase of Bacillus subtilis and structurally characterised with enzymatic and chromatographic techniques. The proportion of large building blocks with a high number of chai...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171234</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171234</guid>        </item>
        <item>
            <title>Applications of β-gal-III isozyme from Bacillus coagulans RCS3, in lactose hydrolysis.</title>
            <link>http://www.medworm.com/index.php?rid=5171233&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21855568%26dopt%3DAbstract</link>
            <description>Authors: Batra N, Singh J, Joshi A, Bhatia S
    Abstract
    Bacillus coagulans RCS3 isolated from hot water springs secreted five isozymes i.e. β-gal I-V of β-galactosidase. β-gal III isozyme was purified using DEAE cellulose and Sephadex G 100 column chromatography. Its molecular weight characterization showed a single band at 315kD in Native PAGE, while two subunits of 50.1 and 53.7kD in SDS PAGE. β-Gal III had pH optima in the range of 6-7 and temperature optima at 65°C. It preferred nitro aryl β-d-galactoside as substrate having K(m) of 4.16mM with ONPG. More than 85% and 80% hydrolysis of lactose (1-5%, w/v) was recorded within 48h of incubation at 55°C and 50°C respectively and pH range of 6-7. About 78-86% hydrolysis of lactose in various brands of standardized milk was re...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5171233</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5171233</guid>        </item>
        <item>
            <title>Impact of intra-subunit interactions on the dimeric arginine kinase activity and structural stability.</title>
            <link>http://www.medworm.com/index.php?rid=5147401&amp;cid=s_35636_60_f&amp;fid=35636&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21839768%26dopt%3DAbstract</link>
            <description>Authors: Wu QY, Jin KZ, Li F, Hu ZQ, Wang XY
    Arginine kinase (AK) catalyzes the reversible phosphorylation of arginine by ATP, yielding the phosphoarginine. In this research, six conserved residues located on the intra-subunit domain-domain interfaces were mutated to explore their roles in the activity and structural stability of dimer AK. The mutations D69A, E70A, E71A and F80A led to pronounced loss of AK activity and structural stability. Although the mutations V75A and F76A had little effect on AK activity and structure, they caused gradually decreased the stability and reactivation of dimer AK. Our results suggested that the mutations might affect the correct positioning of the N-loop and C-loop thus disrupted the efficient recognition and interactions between the N-terminal domai...</description>
            <author>International Journal of Biological Macromolecules</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5147401</comments>
            <pubDate>Thu, 04 Aug 2011 23:00:00 +0100</pubDate>
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